2dc3
From Proteopedia
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| - | [[Image:2dc3.gif|left|200px]]<br /><applet load="2dc3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2dc3, resolution 1.68Å" /> | ||
| - | '''Crystal structure of human cytoglobin at 1.68 angstroms resolution'''<br /> | ||
| - | == | + | ==Crystal structure of human cytoglobin at 1.68 angstroms resolution== |
| + | <StructureSection load='2dc3' size='340' side='right'caption='[[2dc3]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2dc3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DC3 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]] 1.68Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2dc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dc3 OCA], [https://pdbe.org/2dc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2dc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dc3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2dc3 TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYGB_HUMAN CYGB_HUMAN] May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. | ||
| + | == 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/dc/2dc3_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=2dc3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement. | Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement. | ||
| - | + | High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.,Makino M, Sugimoto H, Sawai H, Kawada N, Yoshizato K, Shiro Y Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):671-7. Epub 2006, May 12. PMID:16699195<ref>PMID:16699195</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 2dc3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Kawada | + | [[Category: Kawada N]] |
| - | [[Category: Makino | + | [[Category: Makino M]] |
| - | + | [[Category: Sawai H]] | |
| - | [[Category: Sawai | + | [[Category: Shiro Y]] |
| - | [[Category: Shiro | + | [[Category: Sugimoto H]] |
| - | [[Category: Sugimoto | + | [[Category: Yoshizato K]] |
| - | [[Category: Yoshizato | + | |
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Current revision
Crystal structure of human cytoglobin at 1.68 angstroms resolution
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Categories: Homo sapiens | Large Structures | Kawada N | Makino M | Sawai H | Shiro Y | Sugimoto H | Yoshizato K
