2H92

Crystal Structure of Staphylococcus aureus Cytidine Monophosphate Kinase in complex with cytidine-5'-monophosphate

2H92 の概要

• エントリーDOI: 10.2210/pdb2h92/pdb
• 分子名称: Cytidylate kinase, SULFATE ION, CYTIDINE-5'-MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: rossmann fold, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 75338.99

構造登録者

Dhaliwal, B. (登録日: 2006-06-08, 公開日: 2006-08-08, 最終更新日: 2023-08-30)

主引用文献

Dhaliwal, B.,Ren, J.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K.
Structure of Staphylococcus aureus cytidine monophosphate kinase in complex with cytidine 5'-monophosphate.
Acta Crystallogr.,Sect.F, 62:710-715, 2006

PubMed Abstract: The crystal structure of Staphylococcus aureus cytidine monophosphate kinase (CMK) in complex with cytidine 5'-monophosphate (CMP) has been determined at 2.3 angstroms resolution. The active site reveals novel features when compared with two orthologues of known structure. Compared with the Streptococcus pneumoniae CMK solution structure of the enzyme alone, S. aureus CMK adopts a more closed conformation, with the NMP-binding domain rotating by approximately 16 degrees towards the central pocket of the molecule, thereby assembling the active site. Comparing Escherichia coli and S. aureus CMK-CMP complex structures reveals differences within the active site, including a previously unreported indirect interaction of CMP with Asp33, the replacement of a serine residue involved in the binding of CDP by Ala12 in S. aureus CMK and an additional sulfate ion in the E. coli CMK active site. The detailed understanding of the stereochemistry of CMP binding to CMK will assist in the design of novel inhibitors of the enzyme. Inhibitors are required to treat the widespread hospital infection methicillin-resistant S. aureus (MRSA), currently a major public health concern.

PubMed: 16880539
DOI: 10.1107/S174430910602447X

実験手法

X-RAY DIFFRACTION (2.3 Å)