1ury: Difference between revisions

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[[Image:1ury.gif|left|200px]]<br />
<applet load="1ury" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ury, resolution 2.40&Aring;" />
'''CYTOGLOBIN CAVITIES'''<br />


==About this Structure==
==cytoglobin cavities==
1URY is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with HEM, XE and FC6 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URY OCA]].  
<StructureSection load='1ury' size='340' side='right'caption='[[1ury]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ury]] 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=1URY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URY 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</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=1ury FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ury OCA], [https://pdbe.org/1ury PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ury RCSB], [https://www.ebi.ac.uk/pdbsum/1ury PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ury ProSAT]</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/ur/1ury_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ury ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytoglobin is the fourth recognized globin type, almost ubiquitously distributed in human tissues; its function is still poorly understood. Cytoglobin displays a core region of about 150 residues, structurally related to hemoglobin and myoglobin, and two extra segments, about 20 residues each, at the N- and C-termini. The core region hosts a large apolar cavity, held to provide a ligand diffusion pathway to/from the heme, and/or ligand temporary docking sites. Here we report the crystal structure (2.4A resolution, R-factor 19.1%) of a human cytoglobin mutant bearing the CysB2(38) --&gt; Ser and CysE9(83) --&gt; Ser substitutions (CYGB*), treated under pressurized xenon. Three Xe atoms bind to the heme distal site region of CYGB* mapping the protein matrix apolar cavity. Despite the conserved globin fold, the cavity found in CYGB* is structured differently from those recognized to play a functional role in myoglobin, neuroglobin, truncated hemoglobins, and Cerebratulus lacteus mini-hemoglobin.
 
Mapping protein matrix cavities in human cytoglobin through Xe atom binding.,de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M Biochem Biophys Res Commun. 2004 Apr 16;316(4):1217-21. PMID:15044115<ref>PMID:15044115</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ury" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ascenzi, P.]]
[[Category: Ascenzi P]]
[[Category: Bolognesi, M.]]
[[Category: Bolognesi M]]
[[Category: Burmester, T.]]
[[Category: Burmester T]]
[[Category: Dewilde, S.]]
[[Category: Dewilde S]]
[[Category: Hankeln, T.]]
[[Category: Hankeln T]]
[[Category: Moens, L.]]
[[Category: Moens L]]
[[Category: Pesce, A.]]
[[Category: Pesce A]]
[[Category: Sanctis, D.De.]]
[[Category: De Sanctis D]]
[[Category: FC6]]
[[Category: HEM]]
[[Category: XE]]
[[Category: cytoglobin]]
[[Category: globin]]
[[Category: heme]]
[[Category: hexa-coordination]]
[[Category: histoglobin]]
[[Category: oxygen transport]]
[[Category: protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:09:37 2007''
Retrieved from "https://proteopedia.org/1ury"