Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form

Omar Davulcu; Xiaogang Niu; Lei Brüschweiler-Li; Rafael Brüschweiler; Jack J. Skalicky; Michael S. Chapman

doi:10.1007/s12104-013-9512-4

Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form

Omar Davulcu, Xiaogang Niu, Lei Brüschweiler-Li, Rafael Brüschweiler, Jack J. Skalicky, Michael S. Chapman

Biochemistry & Molecular Biology

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

3 Scopus citations

Abstract

Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with ²H, ¹³C, and ¹⁵N in combination with three enzyme samples prepared with a single ¹⁵N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.

Original language	English (US)
Pages (from-to)	335-338
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	8
Issue number	2
DOIs	https://doi.org/10.1007/s12104-013-9512-4
State	Published - Oct 1 2014

Keywords

Arginine kinase
Enzyme dynamics
NMR spectroscopy
Phosphagen kinase
Resonance assignment
Transition state analogue

ASJC Scopus subject areas

Structural Biology
Biochemistry

Access to Document

10.1007/s12104-013-9512-4

Cite this

@article{a161bf96f7a44344939df82e19503183,

title = "Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form",

abstract = "Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with 2H, 13C, and 15N in combination with three enzyme samples prepared with a single 15N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.",

keywords = "Arginine kinase, Enzyme dynamics, NMR spectroscopy, Phosphagen kinase, Resonance assignment, Transition state analogue",

author = "Omar Davulcu and Xiaogang Niu and Lei Br{\"u}schweiler-Li and Rafael Br{\"u}schweiler and Skalicky, {Jack J.} and Chapman, {Michael S.}",

note = "Publisher Copyright: {\textcopyright} 2013, Springer Science+Business Media Dordrecht.",

year = "2014",

month = oct,

day = "1",

doi = "10.1007/s12104-013-9512-4",

language = "English (US)",

volume = "8",

pages = "335--338",

journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

publisher = "Springer Netherlands",

number = "2",

}

TY - JOUR

T1 - Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form

AU - Davulcu, Omar

AU - Niu, Xiaogang

AU - Brüschweiler-Li, Lei

AU - Brüschweiler, Rafael

AU - Skalicky, Jack J.

AU - Chapman, Michael S.

PY - 2014/10/1

Y1 - 2014/10/1

N2 - Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with 2H, 13C, and 15N in combination with three enzyme samples prepared with a single 15N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.

AB - Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with 2H, 13C, and 15N in combination with three enzyme samples prepared with a single 15N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.

KW - Arginine kinase

KW - Enzyme dynamics

KW - NMR spectroscopy

KW - Phosphagen kinase

KW - Resonance assignment

KW - Transition state analogue

UR - http://www.scopus.com/inward/record.url?scp=84880442644&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84880442644&partnerID=8YFLogxK

U2 - 10.1007/s12104-013-9512-4

DO - 10.1007/s12104-013-9512-4

M3 - Article

C2 - 23893440

AN - SCOPUS:84880442644

SN - 1874-2718

VL - 8

SP - 335

EP - 338

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -