1z47

<StructureSection load='1z47' size='340' side='right' caption='[[1z47]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1z47]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z47 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=405212 ATCC 27009])</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=1z47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z47 OCA], [http://pdbe.org/1z47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z47 RCSB], [http://www.ebi.ac.uk/pdbsum/1z47 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z4/1z47_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

CysA, the ATPase subunit of a putative sulfate ATP-binding cassette transport system of the gram-positive thermoacidophilic bacterium Alicyclobacillus acidocaldarius, was structurally characterized at a resolution of 2.0 Angstroms in the absence of nucleotides. In line with previous findings on ABC-ATPases the structures of the two monomers (called CysA-1 and CysA-2) in the asymmetric unit differ substantially in the arrangement of their individual (sub)domains. CysA-2 was found as a physiological dimer composed of two crystallographically related monomers that are arranged in an open state. Interestingly, while the regulatory domain of CysA-2 packs against its opposing domain that of CysA-1 undergoes a conformational change and, in the dimer, would interfere with the opposing monomer thereby preventing solute translocation. Whether this conformational state is used for regulatory purposes will be discussed.

Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius.,Scheffel F, Demmer U, Warkentin E, Hulsmann A, Schneider E, Ermler U FEBS Lett. 2005 May 23;579(13):2953-8. Epub 2005 Apr 25. PMID:15893314<ref>PMID:15893314</ref>

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

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<div class="pdbe-citations 1z47" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 27009]]

[[Category: Demmer, U]]

[[Category: Ermler, U]]

[[Category: Huelsmann, A]]

[[Category: Scheffel, F]]

[[Category: Schneider, E]]

[[Category: Warkentin, E]]

[[Category: Ligand binding protein]]