Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

Constantina Bakolitsa; Abhinav Kumar; Kevin K. Jin; Daniel McMullan; S. Sri Krishna; Mitchell D. Miller; Polat Abdubek; Claire Acosta; Tamara Astakhova; Herbert L. Axelrod; Prasad Burra; Dennis Carlton; Connie Chen; Hsiu Ju Chiu; Thomas Clayton; Debanu Das; Marc C. Deller; Lian Duan; Ylva Elias; Kyle Ellrott; Dustin Ernst; Carol L. Farr; Julie Feuerhelm; Joanna C. Grant; Anna Grzechnik; Slawomir K. Grzechnik; Gye Won Han; Lukasz Jaroszewski; Hope A. Johnson; Heath E. Klock; Mark W. Knuth; Piotr Kozbial; David Marciano; Andrew T. Morse; Kevin D. Murphy; Edward Nigoghossian; Amanda Nopakun; Linda Okach; Jessica Paulsen; Christina Puckett; Ron Reyes; Christopher L. Rife; Natasha Sefcovic; Henry J. Tien; Christine B. Trame; Christina V. Trout; Henry Van Den Bedem; Dana Weekes; Aprilfawn White; Qingping Xu; Keith O. Hodgson; John Wooley; Marc Andre Elsliger; Ashley M. Deacon; Adam Godzik; Scott A. Lesley; Ian A. Wilson

doi:10.1107/S1744309109050647

Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

Constantina Bakolitsa, Abhinav Kumar, Kevin K. Jin, Daniel McMullan, S. Sri Krishna, Mitchell D. Miller, Polat Abdubek, Claire Acosta, Tamara Astakhova, Herbert L. Axelrod, Prasad Burra, Dennis Carlton, Connie Chen, Hsiu Ju Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Ylva Elias, Kyle EllrottDustin Ernst, Carol L. Farr, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Slawomir K. Grzechnik, Gye Won Han, Lukasz Jaroszewski, Hope A. Johnson, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, David Marciano, Andrew T. Morse, Kevin D. Murphy, Edward Nigoghossian, Amanda Nopakun, Linda Okach, Jessica Paulsen, Christina Puckett, Ron Reyes, Christopher L. Rife, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Christina V. Trout, Henry Van Den Bedem, Dana Weekes, Aprilfawn White, Qingping Xu, Keith O. Hodgson, John Wooley, Marc Andre Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.

Original language	English (US)
Pages (from-to)	1182-1189
Number of pages	8
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	10
DOIs	https://doi.org/10.1107/S1744309109050647
State	Published - Oct 2010
Externally published	Yes

Keywords

amino acids
chorismate mutase
domain of unknown function
pH-dependent
salt-dependent
structural genomics

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309109050647

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Bakolitsa, C., Kumar, A., Jin, K. K., McMullan, D., Krishna, S. S., Miller, M. D., Abdubek, P., Acosta, C., Astakhova, T., Axelrod, H. L., Burra, P., Carlton, D., Chen, C., Chiu, H. J., Clayton, T., Das, D., Deller, M. C., Duan, L., Elias, Y., ... Wilson, I. A. (2010). Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(10), 1182-1189. https://doi.org/10.1107/S1744309109050647

Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism. / Bakolitsa, Constantina; Kumar, Abhinav; Jin, Kevin K. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 10, 10.2010, p. 1182-1189.

Research output: Contribution to journal › Article › peer-review

Bakolitsa, C, Kumar, A, Jin, KK, McMullan, D, Krishna, SS, Miller, MD, Abdubek, P, Acosta, C, Astakhova, T, Axelrod, HL, Burra, P, Carlton, D, Chen, C, Chiu, HJ, Clayton, T, Das, D, Deller, MC, Duan, L, Elias, Y, Ellrott, K, Ernst, D, Farr, CL, Feuerhelm, J, Grant, JC, Grzechnik, A, Grzechnik, SK, Han, GW, Jaroszewski, L, Johnson, HA, Klock, HE, Knuth, MW, Kozbial, P, Marciano, D, Morse, AT, Murphy, KD, Nigoghossian, E, Nopakun, A, Okach, L, Paulsen, J, Puckett, C, Reyes, R, Rife, CL, Sefcovic, N, Tien, HJ, Trame, CB, Trout, CV, Van Den Bedem, H, Weekes, D, White, A, Xu, Q, Hodgson, KO, Wooley, J, Elsliger, MA, Deacon, AM, Godzik, A, Lesley, SA & Wilson, IA 2010, 'Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 66, no. 10, pp. 1182-1189. https://doi.org/10.1107/S1744309109050647

Bakolitsa C, Kumar A, Jin KK, McMullan D, Krishna SS, Miller MD et al. Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2010 Oct;66(10):1182-1189. doi: 10.1107/S1744309109050647

Bakolitsa, Constantina ; Kumar, Abhinav ; Jin, Kevin K. et al. / Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2010 ; Vol. 66, No. 10. pp. 1182-1189.

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abstract = "The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 {\AA} by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.",

keywords = "amino acids, chorismate mutase, domain of unknown function, pH-dependent, salt-dependent, structural genomics",

author = "Constantina Bakolitsa and Abhinav Kumar and Jin, {Kevin K.} and Daniel McMullan and Krishna, {S. Sri} and Miller, {Mitchell D.} and Polat Abdubek and Claire Acosta and Tamara Astakhova and Axelrod, {Herbert L.} and Prasad Burra and Dennis Carlton and Connie Chen and Chiu, {Hsiu Ju} and Thomas Clayton and Debanu Das and Deller, {Marc C.} and Lian Duan and Ylva Elias and Kyle Ellrott and Dustin Ernst and Farr, {Carol L.} and Julie Feuerhelm and Grant, {Joanna C.} and Anna Grzechnik and Grzechnik, {Slawomir K.} and Han, {Gye Won} and Lukasz Jaroszewski and Johnson, {Hope A.} and Klock, {Heath E.} and Knuth, {Mark W.} and Piotr Kozbial and David Marciano and Morse, {Andrew T.} and Murphy, {Kevin D.} and Edward Nigoghossian and Amanda Nopakun and Linda Okach and Jessica Paulsen and Christina Puckett and Ron Reyes and Rife, {Christopher L.} and Natasha Sefcovic and Tien, {Henry J.} and Trame, {Christine B.} and Trout, {Christina V.} and {Van Den Bedem}, Henry and Dana Weekes and Aprilfawn White and Qingping Xu and Hodgson, {Keith O.} and John Wooley and Elsliger, {Marc Andre} and Deacon, {Ashley M.} and Adam Godzik and Lesley, {Scott A.} and Wilson, {Ian A.}",

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doi = "10.1107/S1744309109050647",

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AU - Kumar, Abhinav

AU - Jin, Kevin K.

AU - McMullan, Daniel

AU - Krishna, S. Sri

AU - Miller, Mitchell D.

AU - Abdubek, Polat

AU - Acosta, Claire

AU - Astakhova, Tamara

AU - Axelrod, Herbert L.

AU - Burra, Prasad

AU - Carlton, Dennis

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AU - Chiu, Hsiu Ju

AU - Clayton, Thomas

AU - Das, Debanu

AU - Deller, Marc C.

AU - Duan, Lian

AU - Elias, Ylva

AU - Ellrott, Kyle

AU - Ernst, Dustin

AU - Farr, Carol L.

AU - Feuerhelm, Julie

AU - Grant, Joanna C.

AU - Grzechnik, Anna

AU - Grzechnik, Slawomir K.

AU - Han, Gye Won

AU - Jaroszewski, Lukasz

AU - Johnson, Hope A.

AU - Klock, Heath E.

AU - Knuth, Mark W.

AU - Kozbial, Piotr

AU - Marciano, David

AU - Morse, Andrew T.

AU - Murphy, Kevin D.

AU - Nigoghossian, Edward

AU - Nopakun, Amanda

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AU - Puckett, Christina

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AU - Xu, Qingping

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KW - amino acids

KW - chorismate mutase

KW - domain of unknown function

KW - pH-dependent

KW - salt-dependent

KW - structural genomics

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Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

Abstract

Keywords

ASJC Scopus subject areas

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