1a7e

From Proteopedia

(Difference between revisions)

Revision as of 10:36, 19 May 2021

HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

Structural highlights

1a7e is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HEMTM_THEHE] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms.

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

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a7e"

@@ Line 3: / Line 3: @@
 <StructureSection load='1a7e' size='340' side='right'caption='[[1a7e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7E FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene></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=1a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7e OCA], [http://pdbe.org/1a7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a7e RCSB], [http://www.ebi.ac.uk/pdbsum/1a7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7e ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7e OCA], [https://pdbe.org/1a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7e RCSB], [https://www.ebi.ac.uk/pdbsum/1a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMTM_THEHE HEMTM_THEHE]] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms.
+[[https://www.uniprot.org/uniprot/HEMTM_THEHE HEMTM_THEHE]] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1a7e

From Proteopedia

Revision as of 10:36, 19 May 2021

HYDROXOMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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