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| | ==Crystal Structure of Human Cytoglobin (Ferric Form)== | | ==Crystal Structure of Human Cytoglobin (Ferric Form)== |
| - | <StructureSection load='1v5h' size='340' side='right' caption='[[1v5h]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1v5h' size='340' side='right'caption='[[1v5h]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v5h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V5H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v5h]] is a 1 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=1V5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V5H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYGB, STAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5h OCA], [http://pdbe.org/1v5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v5h RCSB], [http://www.ebi.ac.uk/pdbsum/1v5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v5h ProSAT], [http://www.topsan.org/Proteins/RSGI/1v5h TOPSAN]</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=1v5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5h OCA], [https://pdbe.org/1v5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v5h RCSB], [https://www.ebi.ac.uk/pdbsum/1v5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v5h ProSAT], [https://www.topsan.org/Proteins/RSGI/1v5h TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1v5h" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1v5h" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Cytoglobin|Cytoglobin]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kawada, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Makino, M]] | + | [[Category: Kawada N]] |
| - | [[Category: Structural genomic]] | + | [[Category: Makino M]] |
| - | [[Category: Sawai, H]] | + | [[Category: Sawai H]] |
| - | [[Category: Shiro, Y]] | + | [[Category: Shiro Y]] |
| - | [[Category: Sugimoto, H]] | + | [[Category: Sugimoto H]] |
| - | [[Category: Yoshizato, K]] | + | [[Category: Yoshizato K]] |
| - | [[Category: Globin]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Ligand binding]]
| + | |
| - | [[Category: Oxygen storage]]
| + | |
| - | [[Category: Oxygen storage-transport complex]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
CYGB_HUMAN May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.
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
Cytoglobin (Cgb), a newly discovered member of the vertebrate globin family, binds O(2) reversibly via its heme, as is the case for other mammalian globins (hemoglobin (Hb), myoglobin (Mb) and neuroglobin (Ngb)). While Cgb is expressed in various tissues, its physiological role is not clearly understood. Here, the X-ray crystal structure of wild type human Cgb in the ferric state at 2.4A resolution is reported. In the crystal structure, ferric Cgb is dimerized through two intermolecular disulfide bonds between Cys38(B2) and Cys83(E9), and the dimerization interface is similar to that of lamprey Hb and Ngb. The overall backbone structure of the Cgb monomer exhibits a traditional globin fold with a three-over-three alpha-helical sandwich, in which the arrangement of helices is basically the same among all globins studied to date. A detailed comparison reveals that the backbone structure of the CD corner to D helix region, the N terminus of the E-helix and the F-helix of Cgb resembles more closely those of pentacoordinated globins (Mb, lamprey Hb), rather than hexacoordinated globins (Ngb, rice Hb). However, the His81(E7) imidazole group coordinates directly to the heme iron as a sixth axial ligand to form a hexcoordinated heme, like Ngb and rice Hb. The position and orientation of the highly conserved residues in the heme pocket (Phe(CD1), Val(E11), distal His(E7) and proximal His(F8)) are similar to those of other globin proteins. Two alternative conformations of the Arg84(E10) guanidium group were observed, suggesting that it participates in ligand binding to Cgb, as is the case for Arg(E10) of Aplysia Mb and Lys(E10) of Ngb. The structural diversities and similarities among globin proteins are discussed with relevance to molecular evolutionary relationships.
Structural basis of human cytoglobin for ligand binding.,Sugimoto H, Makino M, Sawai H, Kawada N, Yoshizato K, Shiro Y J Mol Biol. 2004 Jun 11;339(4):873-85. PMID:15165856[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sugimoto H, Makino M, Sawai H, Kawada N, Yoshizato K, Shiro Y. Structural basis of human cytoglobin for ligand binding. J Mol Biol. 2004 Jun 11;339(4):873-85. PMID:15165856 doi:10.1016/j.jmb.2004.04.024
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