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 & 37 others 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

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1182-1189
Number of pages8
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number10
DOIs
StatePublished - Oct 2010
Externally publishedYes

Fingerprint

Chorismate Mutase
Bacillus
metabolism
Bacilli
Metabolism
amino acids
proteins
Amino Acids
National Institute of General Medical Sciences (U.S.)
Proteins
Wavelength
Oligomerization
Environmental regulations
genome
Genomics
oligomers
Oligomers
structural analysis
Structural analysis
wavelengths

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 10, 10.2010, p. 1182-1189.

Research output: Contribution to journalArticle

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, Constantina ; Kumar, Abhinav ; Jin, Kevin K. ; McMullan, Daniel ; Krishna, S. Sri ; Miller, Mitchell D. ; Abdubek, Polat ; Acosta, Claire ; Astakhova, Tamara ; Axelrod, Herbert L. ; Burra, Prasad ; Carlton, Dennis ; Chen, Connie ; Chiu, Hsiu Ju ; Clayton, Thomas ; Das, Debanu ; Deller, Marc C. ; Duan, Lian ; Elias, Ylva ; Ellrott, Kyle ; Ernst, Dustin ; Farr, Carol L. ; Feuerhelm, Julie ; Grant, Joanna C. ; Grzechnik, Anna ; Grzechnik, Slawomir K. ; Han, Gye Won ; Jaroszewski, Lukasz ; Johnson, Hope A. ; Klock, Heath E. ; Knuth, Mark W. ; Kozbial, Piotr ; Marciano, David ; Morse, Andrew T. ; Murphy, Kevin D. ; Nigoghossian, Edward ; Nopakun, Amanda ; Okach, Linda ; Paulsen, Jessica ; Puckett, Christina ; Reyes, Ron ; Rife, Christopher L. ; Sefcovic, Natasha ; Tien, Henry J. ; Trame, Christine B. ; Trout, Christina V. ; Van Den Bedem, Henry ; Weekes, Dana ; White, Aprilfawn ; Xu, Qingping ; Hodgson, Keith O. ; Wooley, John ; Elsliger, Marc Andre ; Deacon, Ashley M. ; Godzik, Adam ; Lesley, Scott A. ; Wilson, Ian A. / 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.",
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T1 - 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

AU - Bakolitsa, Constantina

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

AU - Chen, Connie

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

AU - Okach, Linda

AU - Paulsen, Jessica

AU - Puckett, Christina

AU - Reyes, Ron

AU - Rife, Christopher L.

AU - Sefcovic, Natasha

AU - Tien, Henry J.

AU - Trame, Christine B.

AU - Trout, Christina V.

AU - Van Den Bedem, Henry

AU - Weekes, Dana

AU - White, Aprilfawn

AU - Xu, Qingping

AU - Hodgson, Keith O.

AU - Wooley, John

AU - Elsliger, Marc Andre

AU - Deacon, Ashley M.

AU - Godzik, Adam

AU - Lesley, Scott A.

AU - Wilson, Ian A.

PY - 2010/10

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N2 - 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.

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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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