1a7e: Difference between revisions

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<StructureSection load='1a7e' size='340' side='right'caption='[[1a7e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1a7e' size='340' side='right'caption='[[1a7e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== 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 [https://proteopedia.org/fgij/fg.htm?mol=1A7E FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_hennahi Themiste hennahi]. 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" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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'>[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>
<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>
</table>
== Function ==
== Function ==
[[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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7e ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7e ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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., &amp; 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<ref>PMID:9188702</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a7e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hill, C P]]
[[Category: Themiste hennahi]]
[[Category: Junior, W R.Ellis]]
[[Category: Ellis Junior WR]]
[[Category: Martins, L J]]
[[Category: Hill CP]]
[[Category: Nonheme iron oxygen carrier]]
[[Category: Martins LJ]]
[[Category: Oxygen transport]]

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