2J41

Crystal structure of Staphylococcus aureus guanylate monophosphate kinase

2J41 の概要

• エントリーDOI: 10.2210/pdb2j41/pdb
• 分子名称: GUANYLATE KINASE, SULFATE ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: gmp, gmk, kinase, transferase, atp-binding, nucleotide-binding, staphylococcus aureus
• 由来する生物種: STAPHYLOCOCCUS AUREUS
• 細胞内の位置: Cytoplasm (By similarity): Q5HGM3
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 97980.94

構造登録者

El Omari, K.,Dhaliwal, B.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K. (登録日: 2006-08-24, 公開日: 2006-10-11, 最終更新日: 2024-10-23)

主引用文献

El Omari, K.,Dhaliwal, B.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K.
Structure of Staphylococcus Aureus Guanylate Monophosphate Kinase
Acta Crystallogr.,Sect.F, 62:949-, 2006

PubMed Abstract: Nucleotide monophosphate kinases (NMPKs) are potential antimicrobial drug targets owing to their role in supplying DNA and RNA precursors. The present work reports the crystal structure of Staphylococcus aureus guanylate monophosphate kinase (SaGMK) at 1.9 A resolution. The structure shows that unlike most GMKs SaGMK is dimeric, confirming the role of the extended C-terminus in dimer formation as first observed for Escherichia coli GMK (EcGMK). One of the two SaGMK dimers within the crystal asymmetric unit has two monomers in different conformations: an open form with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a closed form with bound GMP and sulfate ion. GMP-induced domain movements in SaGMK can thus be defined by comparison of these conformational states. Like other GMKs, the binding of GMP firstly triggers a partial closure of the enzyme, diminishing the distance between the GMP-binding and ATP-binding sites. In addition, the closed structure shows the presence of a potassium ion in contact with the guanine ring of GMP. The potassium ion appears to form an integral part of the GMP-binding site, as the Tyr36 side chain has significantly moved to form a metal ion-ligand coordination involving the lone pair of the side-chain O atom. The potassium-binding site might also be exploited in the design of novel inhibitors.

PubMed: 17012781
DOI: 10.1107/S174430910603613X

実験手法

X-RAY DIFFRACTION (1.9 Å)