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PDBsum entry 3ewk

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protein ligands metals links
Flavoprotein PDB id
3ewk
Jmol PyMol
Contents
Protein chain
227 a.a. *
Ligands
FAD
GOL
Metals
_CL
Waters ×59
* Residue conservation analysis
PDB id:
3ewk
Name: Flavoprotein
Title: Structure of the redox sensor domain of methylococcus capsul (bath) mmos
Structure: Sensor protein. Chain: a. Fragment: fad(99-325). Engineered: yes
Source: Methylococcus capsulatus. Organism_taxid: 414. Gene: mca1204, mmos. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.34Å     R-factor:   0.240     R-free:   0.283
Authors: U.E.Ukaegbu,A.C.Rosenzweig
Key ref: U.E.Ukaegbu and A.C.Rosenzweig (2009). Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS. Biochemistry, 48, 2207-2215. PubMed id: 19271777
Date:
15-Oct-08     Release date:   24-Mar-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q609M8  (Q609M8_METCA) -  Sensory box histidine kinase/response regulator
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1177 a.a.
227 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.13.3  - Histidine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
ATP
+ protein L-histidine
=
ADP
Bound ligand (Het Group name = FAD)
matches with 50.94% similarity
+ protein N-phospho-L-histidine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochemistry 48:2207-2215 (2009)
PubMed id: 19271777  
 
 
Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS.
U.E.Ukaegbu, A.C.Rosenzweig.
 
  ABSTRACT  
 
MmoS from Methylococcus capsulatus (Bath) is the multidomain sensor protein of a two-component signaling system proposed to play a role in the copper-mediated regulation of soluble methane monooxygenase (sMMO). MmoS binds an FAD cofactor within its N-terminal tandem Per-Arnt-Sim (PAS) domains, suggesting that it functions as a redox sensor. The crystal structure of the MmoS tandem PAS domains, designated PAS-A and PAS-B, has been determined to 2.34 A resolution. Both domains adopt the typical PAS domain alpha/beta topology and are structurally similar. The two domains are linked by a long alpha helix and do not interact with one another. The FAD cofactor is housed solely within PAS-A and is stabilized by an extended hydrogen bonding network. The overall fold of PAS-A is similar to those of other flavin-containing PAS domains, but homodimeric interactions in other structures are not observed in the MmoS sensor, which crystallized as a monomer. The structure both provides new insight into the architecture of tandem PAS domains and suggests specific residues that may play a role in MmoS FAD redox chemistry and subsequent signal transduction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21028987 D.F.Becker, W.Zhu, and M.A.Moxley (2011).
Flavin redox switching of protein functions.
  Antioxid Redox Signal, 14, 1079-1091.  
20545849 A.J.Campbell, K.J.Watts, M.S.Johnson, and B.L.Taylor (2010).
Gain-of-function mutations cluster in distinct regions associated with the signalling pathway in the PAS domain of the aerotaxis receptor, Aer.
  Mol Microbiol, 77, 575-586.  
20223701 J.Cheung, and W.A.Hendrickson (2010).
Sensor domains of two-component regulatory systems.
  Curr Opin Microbiol, 13, 116-123.  
19906177 P.Slavny, R.Little, P.Salinas, T.A.Clarke, and R.Dixon (2010).
Quaternary structure changes in a second Per-Arnt-Sim domain mediate intramolecular redox signal relay in the NifL regulatory protein.
  Mol Microbiol, 75, 61-75.  
20825354 T.Krell, J.Lacal, A.Busch, H.Silva-Jiménez, M.E.Guazzaroni, and J.L.Ramos (2010).
Bacterial sensor kinases: diversity in the recognition of environmental signals.
  Annu Rev Microbiol, 64, 539-559.  
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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