2jcg: Difference between revisions
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[[Image: | ==APO FORM OF THE CATABOLITE CONTROL PROTEIN A (CCPA) FROM BACILLUS MEGATERIUM, WITH THE DNA BINDING DOMAIN== | ||
<StructureSection load='2jcg' size='340' side='right' caption='[[2jcg]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
[[2jcg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JCG OCA]. <br> | |||
<b>Related:</b> [[1rzr|1rzr]], [[1sxg|1sxg]], [[1sxh|1sxh]], [[1sxi|1sxi]], [[1zvv|1zvv]]<br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jc/2jcg_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> | |||
== Publication Abstract from PubMed == | |||
Crystal structure determination of catabolite control protein A (CcpA) at 2.6 A resolution reveals for the first time the structure of a full-length apo-form LacI-GalR family repressor protein. In the crystal structures of these transcription regulators, the three-helix bundle of the DNA-binding domain has only been observed in cognate DNA complexes; it has not been observed in other crystal structures owing to its mobility. In the crystal packing of apo-CcpA, the protein-protein contacts between the N-terminal three-helix bundle and the core domain consisted of interactions between the homodimers that were similar to those between the corepressor protein HPr and the CcpA N-subdomain in the ternary DNA complex. In contrast to the DNA complex, the apo-CcpA structure reveals large subdomain movements in the core, resulting in a complete loss of contacts between the N-subdomains of the homodimer. | |||
Structure of the apo form of the catabolite control protein A (CcpA) from Bacillus megaterium with a DNA-binding domain.,Singh RK, Palm GJ, Panjikar S, Hinrichs W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):253-7. Epub 2007 Mar 12. PMID:17401189<ref>PMID:17401189</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Hinrichs, W.]] | [[Category: Hinrichs, W.]] | ||
Revision as of 08:22, 30 April 2014
APO FORM OF THE CATABOLITE CONTROL PROTEIN A (CCPA) FROM BACILLUS MEGATERIUM, WITH THE DNA BINDING DOMAIN
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