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PDBsum entry 2qhs

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protein ligands links
Transferase PDB id
2qhs

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
210 a.a. *
Ligands
OCA
Waters ×380
* Residue conservation analysis
PDB id:
2qhs
Name: Transferase
Title: Structural basis of octanoic acid recognition by lipoate-protein ligase b
Structure: Lipoyltransferase. Chain: a. Synonym: lipb, lipoyl-[acyl-carrier-protein]-protein- n- lipoyltransferase, lipoate-protein ligase b. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Gene: ttc 1746. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.50Å     R-factor:   0.187     R-free:   0.208
Authors: D.J.Kim,S.J.Lee,H.S.Kim,K.H.Kim,H.H.Lee,H.J.Yoon,S.W.Suh
Key ref:
d.o. .J.Kim et al. (2008). Structural basis of octanoic acid recognition by lipoate-protein ligase B. Proteins, 70, 1620-1625. PubMed id: 18076036 DOI: 10.1002/prot.21843
Date:
02-Jul-07     Release date:   26-Feb-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5SLQ3  (LIPB_THET8) -  Octanoyltransferase from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
217 a.a.
210 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.181  - lipoyl(octanoyl) transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: octanoyl-[ACP] + L-lysyl-[protein] = N6-octanoyl-L-lysyl-[protein] + holo-[ACP] + H+
octanoyl-[ACP]
Bound ligand (Het Group name = OCA)
matches with 75.00% similarity
+ L-lysyl-[protein]
= N(6)-octanoyl-L-lysyl-[protein]
+ holo-[ACP]
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1002/prot.21843 Proteins 70:1620-1625 (2008)
PubMed id: 18076036  
 
 
Structural basis of octanoic acid recognition by lipoate-protein ligase B.
d.o. .J.Kim, S.J.Lee, H.S.Kim, K.H.Kim, H.H.Lee, H.J.Yoon, S.W.Suh.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Overall fold and topology diagram of Tth LipB. (A) F[o] - F[c] electron density maps of the bound ligands contoured at 1.8 . Atoms of the ligands are also labeled. All the figures are drawn with PyMOL (DeLano, 2002, The PyMOL Molecular Graphics System, http://www.pymol.org/). (B) Ribbon diagram. Secondary structure elements were assigned by PROMOTIF.[19] -Helices, -strands, and loops are colored in cyan, yellow, and pink, respectively. Octanoic acid bound near the center of LipB is shown in sticks.
Figure 2.
Figure 2. Octanoic acid binding to Tth LipB. (A) Stereo view of the active site around the bound octanoic acid. Black dotted lines denote hydrogen bonds (B) Ribbon diagram of the crystal structure of Mtu LipB[11] and the homology model of E. coli LipB. -Helices, -strands, and loops are colored in cyan, yellow, and pink, respectively. Decanoic acid and octanoic acid bound to each of the two proteins are shown in sticks.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 70, 1620-1625) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19520844 Q.H.Christensen, and J.E.Cronan (2009).
The Thermoplasma acidophilum LplA-LplB Complex Defines a New Class of Bipartite Lipoate-protein Ligases.
  J Biol Chem, 284, 21317-21326.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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