PMID- 17525466
OWN - NLM
STAT- MEDLINE
DCOM- 20070716
LR  - 20181227
IS  - 0961-8368 (Print)
IS  - 1469-896X (Electronic)
IS  - 0961-8368 (Linking)
VI  - 16
IP  - 6
DP  - 2007 Jun
TI  - Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal 
      structure and its interaction with acyl carrier protein.
PG  - 1184-92
AB  - Malonyl-CoA: acyl carrier protein transacylase (MCAT) is a critical enzyme 
      responsible for the transfer of the malonyl moiety to holo-acyl carrier protein 
      (ACP) forming the malonyl-ACP intermediates in the initiation step of type II 
      fatty acid synthesis (FAS II) in bacteria. MCAT has been considered as an 
      attractive drug target in the discovery of antibacterial agents. In this study, 
      the crystal structure of MCAT from Helicobacter pylori (Hp) at 2.5 angstroms 
      resolution is reported, and the interaction of HpMCAT with HpACP is extensively 
      investigated by using computational docking, GST-pull-down, and surface plasmon 
      resonance (SPR) technology-based assays. The crystal structure results reveal 
      that HpMCAT has a compact folding composed of a large subdomain with a similar 
      core as in alpha/beta hydrolases, and a similar ferredoxin-like small subdomain 
      as in acylphosphatases. The docking result suggests two positively charged areas 
      near the entrance of the active site of HpMCAT as the ACP-binding region. Binding 
      assay research shows that HpMCAT demonstrates a moderately binding ability 
      against HpACP. The solved 3D structure of HpMCAT is expected to supply useful 
      information for the structure-based discovery of novel inhibitors against MCAT, 
      and the quantitative study of HpMCAT interaction with HpACP is hoped to give 
      helpful hints in the understanding of the detailed catalytic mechanisms for 
      HpMCAT.
FAU - Zhang, Liang
AU  - Zhang L
AD  - Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai 
      Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
FAU - Liu, Weizhi
AU  - Liu W
FAU - Xiao, Jianfeng
AU  - Xiao J
FAU - Hu, Tiancen
AU  - Hu T
FAU - Chen, Jing
AU  - Chen J
FAU - Chen, Kaixian
AU  - Chen K
FAU - Jiang, Hualiang
AU  - Jiang H
FAU - Shen, Xu
AU  - Shen X
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Protein Sci
JT  - Protein science : a publication of the Protein Society
JID - 9211750
RN  - 0 (Bacterial Proteins)
RN  - EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase)
SB  - IM
MH  - Acyl-Carrier Protein S-Malonyltransferase/chemistry/genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/genetics/*metabolism
MH  - Binding Sites
MH  - Crystallography, X-Ray/methods
MH  - Helicobacter pylori/*enzymology/genetics
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
PMC - PMC2206670
EDAT- 2007/05/26 09:00
MHDA- 2007/07/17 09:00
PMCR- 2007/06/01
CRDT- 2007/05/26 09:00
PHST- 2007/05/26 09:00 [pubmed]
PHST- 2007/07/17 09:00 [medline]
PHST- 2007/05/26 09:00 [entrez]
PHST- 2007/06/01 00:00 [pmc-release]
AID - 16/6/1184 [pii]
AID - 1184 [pii]
AID - 10.1110/ps.072757307 [doi]
PST - ppublish
SO  - Protein Sci. 2007 Jun;16(6):1184-92. doi: 10.1110/ps.072757307.