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PDBsum entry 1a7d

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protein ligands metals links
Oxygen transport PDB id
1a7d

 

 

 

 

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Contents
Protein chain
118 a.a. *
Ligands
CFO
Metals
_CL ×2
Waters ×666
* Residue conservation analysis
PDB id:
1a7d
Name: Oxygen transport
Title: Chloromet myohemerythrin from themiste zostericola
Structure: Myohemerythrin. Chain: a. Engineered: yes. Other_details: contains a chloro-diiron-oxo (fe1-o-fe2) moiety (cfo).
Source: Themiste zostericola. Organism_taxid: 6437. Cell_line: bl21. Tissue: retractor muscles. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.80Å     R-factor:   0.180     R-free:   0.227
Authors: L.J.Martins,C.P.Hill,W.R.Ellis Junior
Key ref:
L.J.Martins et al. (1997). Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution. Biochemistry, 36, 7044-7049. PubMed id: 9188702 DOI: 10.1021/bi9630422
Date:
12-Mar-98     Release date:   14-Oct-98    
PROCHECK
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 Headers
 References

Protein chain
P02247  (HEMTM_THEHE) -  Myohemerythrin from Themiste hennahi
Seq:
Struc:
118 a.a.
118 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1021/bi9630422 Biochemistry 36:7044-7049 (1997)
PubMed id: 9188702  
 
 
Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.
L.J.Martins, C.P.Hill, W.R.Ellis.
 
  ABSTRACT  
 
Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor muscles of marine "peanut" worms. The X-ray crystal structures of two recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A. Surprisingly, the met wild-type structure (R = 17.8%) was found to contain chloride bound to Fe2, while coordinated hydroxide was found in the met L103N structure (R = 18.3%). An internal water molecule was also found distal to the Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent with the kinetic and spectroscopic results reported for the L103N mutant Mhr [Raner, G. M., Martins, L. J., & Ellis, W. R., Jr. (1997) Biochemistry 36, 7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type Mhr) in gating ligand binding are also discussed.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19691327 J.A.Larrabee, W.R.Johnson, and A.S.Volwiler (2009).
Magnetic circular dichroism study of a dicobalt(II) complex with mixed 5- and 6-coordination: a spectroscopic model for dicobalt(II) hydrolases.
  Inorg Chem, 48, 8822-8829.  
15885093 O.A.Karlsen, L.Ramsevik, L.J.Bruseth, Ã.˜.Larsen, A.Brenner, F.S.Berven, H.B.Jensen, and J.R.Lillehaug (2005).
Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath).
  FEBS J, 272, 2428-2440.  
15341736 V.Adam, A.Royant, V.Nivière, F.P.Molina-Heredia, and D.Bourgeois (2004).
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.
  Structure, 12, 1729-1740.
PDB codes: 1vzg 1vzh 1vzi
11500872 M.Merkx, D.A.Kopp, M.H.Sazinsky, J.L.Blazyk, J.Müller, and S.J.Lippard (2001).
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
  Angew Chem Int Ed Engl, 40, 2782-2807.  
10913259 J.Xiong, R.S.Phillips, D.M.Kurtz, S.Jin, J.Ai, and J.Sanders-Loehr (2000).
The O(2) binding pocket of myohemerythrin: role of a conserved leucine.
  Biochemistry, 39, 8526-8536.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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