PDBsum entry 2h1y

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protein Protein-protein interface(s) links
Transferase PDB id
Protein chains
310 a.a. *
Waters ×26
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of malonyl-coa:acyl carrier protein transa (mcat) from helicobacter pylori
Structure: Malonyl coenzyme a-acyl carrier protein transacyl chain: a, b. Synonym: mcat, malonyl-coa:acyl carrier protein transacylas engineered: yes
Source: Helicobacter pylori. Organism_taxid: 102617. Strain: ss1. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.50Å     R-factor:   0.215     R-free:   0.262
Authors: L.Zhang,W.Liu,X.Shen,H.Jiang
Key ref:
L.Zhang et al. (2007). Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein. Protein Sci, 16, 1184-1192. PubMed id: 17525466 DOI: 10.1110/ps.072757307
17-May-06     Release date:   22-May-07    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q56S05  (Q56S05_HELPX) -  Malonyl CoA-acyl carrier protein transacylase
309 a.a.
310 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - [Acyl-carrier-protein] S-malonyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein]
+ [acyl-carrier-protein]
= CoA
+ malonyl-[acyl-carrier- protein]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     catalytic activity     4 terms  


DOI no: 10.1110/ps.072757307 Protein Sci 16:1184-1192 (2007)
PubMed id: 17525466  
Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein.
L.Zhang, W.Liu, J.Xiao, T.Hu, J.Chen, K.Chen, H.Jiang, X.Shen.
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 A 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.
  Selected figure(s)  
Figure 2.
Figure 2. (A) The topology diagram of HpMCAT. (Cylinders) Helices; (arrows) strands. The alignment was produced by the topology cartoon server from
Figure 4.
Figure 4. H-bond network around the active site. Atoms are shown as
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1184-1192) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19549604 G.Bunkoczi, S.Misquitta, X.Wu, W.H.Lee, A.Rojkova, G.Kochan, K.L.Kavanagh, U.Oppermann, and S.Smith (2009).
Structural basis for different specificities of acyltransferases associated with the human cytosolic and mitochondrial fatty acid synthases.
  Chem Biol, 16, 667-675.  
  17909282 H.Ghadbane, A.K.Brown, L.Kremer, G.S.Besra, and K.Fütterer (2007).
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 831-835.
PDB code: 2qj3
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