1a7d: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Themiste_hennahi Themiste hennahi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Themiste_hennahi Themiste hennahi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7D FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [http://www.ebi.ac.uk/pdbsum/1a7d PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [http://www.ebi.ac.uk/pdbsum/1a7d PDBsum]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Themiste hennahi]]
[[Category: Themiste hennahi]]
[[Category: Hill, C P.]]
[[Category: Hill, C P]]
[[Category: Junior, W R.Ellis.]]
[[Category: Junior, W R.Ellis]]
[[Category: Martins, L J.]]
[[Category: Martins, L J]]
[[Category: Nonheme iron oxygen carrier]]
[[Category: Nonheme iron oxygen carrier]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]

Revision as of 12:12, 22 December 2014

CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLACHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

Structural highlights

1a7d is a 1 chain structure with sequence from Themiste hennahi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Martins LJ, Hill CP, Ellis WR Jr. Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution. Biochemistry. 1997 Jun 10;36(23):7044-9. PMID:9188702 doi:10.1021/bi9630422

1a7d, resolution 1.80Å

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