1a7e

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|PDB= 1a7e |SIZE=350|CAPTION= <scene name='initialview01'>1a7e</scene>, resolution 1.8&Aring;
|PDB= 1a7e |SIZE=350|CAPTION= <scene name='initialview01'>1a7e</scene>, resolution 1.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=OFO:HYDROXY DIIRON-OXO MOIETY'>OFO</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7e OCA], [http://www.ebi.ac.uk/pdbsum/1a7e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a7e RCSB]</span>
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[[Category: Junior, W R.Ellis.]]
[[Category: Junior, W R.Ellis.]]
[[Category: Martins, L J.]]
[[Category: Martins, L J.]]
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[[Category: CL]]
 
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[[Category: OFO]]
 
[[Category: nonheme iron oxygen carrier]]
[[Category: nonheme iron oxygen carrier]]
[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:53 2008''

Revision as of 15:34, 30 March 2008


PDB ID 1a7e

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA


Overview

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.

About this Structure

1A7E is a Single protein structure of sequence from Themiste zostericola. Full crystallographic information is available from OCA.

Reference

Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution., Martins LJ, Hill CP, Ellis WR Jr, Biochemistry. 1997 Jun 10;36(23):7044-9. PMID:9188702

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