2hmq
From Proteopedia
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| - | [[Image:2hmq.gif|left|200px]] | ||
| - | < | + | ==THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION== |
| - | + | <StructureSection load='2hmq' size='340' side='right'caption='[[2hmq]], [[Resolution|resolution]] 1.66Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2hmq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmq 1hmq], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmm 1hmm] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmn 1hmn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HMQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</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=2hmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmq OCA], [https://pdbe.org/2hmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hmq RCSB], [https://www.ebi.ac.uk/pdbsum/2hmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmq ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms. | |
| - | + | == Evolutionary Conservation == | |
| - | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/2hmq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2hmq ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact. | The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact. | ||
| - | + | Structures of met and azidomet hemerythrin at 1.66 A resolution.,Holmes MA, Stenkamp RE J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128<ref>PMID:1870128</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2hmq" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Themiste dyscritum]] | [[Category: Themiste dyscritum]] | ||
| - | [[Category: Holmes | + | [[Category: Holmes MA]] |
| - | [[Category: Stenkamp | + | [[Category: Stenkamp RE]] |
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| - | + | ||
Current revision
THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION
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