4rvc

</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=4rvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rvc OCA], [https://pdbe.org/4rvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rvc RCSB], [https://www.ebi.ac.uk/pdbsum/4rvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rvc ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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