4rvc: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Structure of ATP binding subunit of ABC transporter== | ||
<StructureSection load='4rvc' size='340' side='right' caption='[[4rvc]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rvc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RVC FirstGlance]. <br> | |||
</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=4rvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rvc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rvc RCSB], [http://www.ebi.ac.uk/pdbsum/4rvc PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ATP binding cassette (ABC) transporters, represent one of the largest superfamilies of primary transporters, which are very essential for various biological functions. The crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus has been determined at 1.77 A resolution. The crystal structure revealed that the protomer has two thick arms, (arm I and II), which resemble 'L' shape. The ATP-binding pocket is located close to the end of arm I. ATP molecule is docked into the active site of the protein. The dimeric crystal structure of ATP-binding subunit of ABC transporter from G. kaustophilus has been compared with the previously reported crystal structure of ATP-binding subunit of ABC transporter from Salmonella typhimurium. | |||
Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus.,Manjula M, Pampa KJ, Kumar SM, Mukherjee S, Kunishima N, Rangappa KS, Lokanath NK Biochem Biophys Res Commun. 2015 Mar 27;459(1):113-7. doi:, 10.1016/j.bbrc.2015.02.079. Epub 2015 Feb 25. PMID:25724946<ref>PMID:25724946</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
[[Category: Lokanath, N | </StructureSection> | ||
[[Category: Lokanath, N K]] | |||
[[Category: Manjula, M]] | [[Category: Manjula, M]] | ||
[[Category: Pampa, K J]] | |||
[[Category: Atp bindig]] | |||
[[Category: Motif c]] | |||
[[Category: Transport protein]] | |||
Revision as of 12:07, 18 March 2015
Structure of ATP binding subunit of ABC transporter
| ||||||||||||