4e89: Difference between revisions
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[[ | ==Crystal Structure of RnaseH from gammaretrovirus== | ||
<StructureSection load='4e89' size='340' side='right' caption='[[4e89]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e89]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenotropic_mulv-related_virus_vp62 Xenotropic mulv-related virus vp62]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E89 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </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=4e89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e89 RCSB], [http://www.ebi.ac.uk/pdbsum/4e89 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA. In the present study we have determined the complete structure of the RNase H domain from XMRV (xenotropic murine leukaemia virus-related virus) RT (reverse transcriptase). The basic protrusion motif of the XMRV RNase H domain is folded as a short helix and an adjacent highly bent loop. Structural superposition and subsequent mutagenesis experiments suggest that the basic protrusion motif plays a role in direct binding to the major groove in RNA/DNA hybrid, as well as in establishing the co-ordination among modules in RT necessary for proper function. | |||
Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.,Kim JH, Kang S, Jung SK, Yu KR, Chung SJ, Chung BH, Erikson RL, Kim BY, Kim SJ Biosci Rep. 2012 Oct 1;32(5):455-63. PMID:22724525<ref>PMID:22724525</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Ribonuclease|Ribonuclease]] | |||
== | *[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]] | ||
[[ | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Xenotropic mulv-related virus vp62]] | [[Category: Xenotropic mulv-related virus vp62]] | ||
[[Category: Kim, J H | [[Category: Kim, J H]] | ||
[[Category: Kim, S J | [[Category: Kim, S J]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||