4QTO

1.65 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus with BME-modified Cys289 and PEG molecule in active site

4QTO の概要

• エントリーDOI: 10.2210/pdb4qto/pdb
• 関連するPDBエントリー: 4MPB 4MPY 4NEA 4NU9 4Q92 4QJE 4QN2
• 分子名称: Betaine aldehyde dehydrogenase, SODIUM ION, TRIETHYLENE GLYCOL, ... (8 entities in total)
• 機能のキーワード: betb, structural genomics, nad, niaid, national institute of allergy and infectious diseases, csgid, rossmann fold, center for structural genomics of infectious diseases, oxidoreductase
• 由来する生物種: Staphylococcus aureus subsp. aureus COL
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 231998.45

構造登録者

Halavaty, A.S.,Minasov, G.,Dubrovska, I.,Winsor, J.,Shuvalova, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2014-07-08, 公開日: 2014-07-16, 最終更新日: 2024-11-20)

主引用文献

Halavaty, A.S.,Rich, R.L.,Chen, C.,Joo, J.C.,Minasov, G.,Dubrovska, I.,Winsor, J.R.,Myszka, D.G.,Duban, M.,Shuvalova, L.,Yakunin, A.F.,Anderson, W.F.
Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus.
Acta Crystallogr.,Sect.D, 71:1159-1175, 2015

PubMed Abstract: When exposed to high osmolarity, methicillin-resistant Staphylococcus aureus (MRSA) restores its growth and establishes a new steady state by accumulating the osmoprotectant metabolite betaine. Effective osmoregulation has also been implicated in the acquirement of a profound antibiotic resistance by MRSA. Betaine can be obtained from the bacterial habitat or produced intracellularly from choline via the toxic betaine aldehyde (BA) employing the choline dehydrogenase and betaine aldehyde dehydrogenase (BADH) enzymes. Here, it is shown that the putative betaine aldehyde dehydrogenase SACOL2628 from the early MRSA isolate COL (SaBADH) utilizes betaine aldehyde as the primary substrate and nicotinamide adenine dinucleotide (NAD(+)) as the cofactor. Surface plasmon resonance experiments revealed that the affinity of NAD(+), NADH and BA for SaBADH is affected by temperature, pH and buffer composition. Five crystal structures of the wild type and three structures of the Gly234Ser mutant of SaBADH in the apo and holo forms provide details of the molecular mechanisms of activity and substrate specificity/inhibition of this enzyme.

PubMed: 25945581
DOI: 10.1107/S1399004715004228

実験手法

X-RAY DIFFRACTION (1.65 Å)