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1a7e
From Proteopedia
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|PDB= 1a7e |SIZE=350|CAPTION= <scene name='initialview01'>1a7e</scene>, resolution 1.8Å | |PDB= 1a7e |SIZE=350|CAPTION= <scene name='initialview01'>1a7e</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Junior, W R.Ellis.]] | [[Category: Junior, W R.Ellis.]] | ||
[[Category: Martins, L J.]] | [[Category: Martins, L J.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: OFO]] | ||
[[Category: nonheme iron oxygen carrier]] | [[Category: nonheme iron oxygen carrier]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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| , 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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