1a7e
From Proteopedia
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- | [[Image:1a7e.gif|left|200px]] | + | [[Image:1a7e.gif|left|200px]] |
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- | '''HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA''' | + | {{Structure |
+ | |PDB= 1a7e |SIZE=350|CAPTION= <scene name='initialview01'>1a7e</scene>, resolution 1.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=OFO:HYDROXY DIIRON-OXO MOIETY'>OFO</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1A7E is a [ | + | 1A7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_zostericola Themiste zostericola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7E OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9188702 9188702] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Themiste zostericola]] | [[Category: Themiste zostericola]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:59 2008'' |
Revision as of 07:54, 20 March 2008
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, resolution 1.8Å | |||||||
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Ligands: | and | ||||||
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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