3ahs: Difference between revisions
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[[Image: | ==Crystal Structure of Ustilago sphaerogena Ribonuclease U2B== | ||
<StructureSection load='3ahs' size='340' side='right' caption='[[3ahs]], [[Resolution|resolution]] 1.32Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ahs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ustilago_sphaerogena Ustilago sphaerogena]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AHS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agn|3agn]], [[3ago|3ago]], [[1rtu|1rtu]], [[3ahw|3ahw]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_U(2) Ribonuclease U(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.4 3.1.27.4] </span></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=3ahs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ahs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ahs RCSB], [http://www.ebi.ac.uk/pdbsum/3ahs PDBsum]</span></td></tr> | |||
</table> | |||
== 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/ah/3ahs_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Under physiological conditions, the deamidation and isomerization of asparagine to isoaspartate (isoAsp) proceeds non-enzymatically via succinimide. Although a large number of proteins have been reported to contain isoAsp, information concerning the three-dimensional structure of proteins containing isoaspartate is still limited. We have crystallized isoAsp containing Ustilago sphaerogena ribonuclease U2B, and determined the crystal structure at 1.32 A resolution. The structure revealed that the formation of isoAsp32 induces a single turn unfolding of the alpha-helix from Asp29 to Asp34, and the region from Asp29 to Arg35 forms a U-shaped loop structure. The electron density map shows that isoAsp32 retained the l-configuration at the C(alpha) atom. IsoAsp32 is in gauche conformation about a C(alpha)-C(beta) bond, and the polypeptide chain bends by approximately 90 degrees at isoAsp32. IsoAsp32 protrudes from the surface of the protein, and the abnormal beta-peptide bond in the main-chain and alpha-carboxylate in the side-chain is fully exposed. The structure suggests that the deamidation of the Asn and the isoAsp formation in proteins could confer immunogenicity. (c) 2010 Wiley Periodicals, Inc. Biopolymers, 2010. | |||
Structural changes induced by the deamidation and isomerization of asparagine revealed by the crystal structure of Ustilago sphaerogena ribonuclease U2B.,Noguchi S Biopolymers. 2010 Jul 8. PMID:20623666<ref>PMID:20623666</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease|Ribonuclease]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Ustilago sphaerogena]] | [[Category: Ustilago sphaerogena]] | ||
[[Category: Noguchi, S.]] | [[Category: Noguchi, S.]] | ||