PDBsum entry 3ewk

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Flavoprotein PDB id
Jmol PyMol
Protein chain
227 a.a. *
Waters ×59
* Residue conservation analysis
PDB id:
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.
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
15-Oct-08     Release date:   24-Mar-09    
Go to PROCHECK summary

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

 Enzyme reactions 
   Enzyme class: E.C.  - Histidine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
+ protein L-histidine
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


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.
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.  
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