2m8c: Difference between revisions
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==The solution NMR structure of E. coli apo-HisJ== | ==The solution NMR structure of E. coli apo-HisJ== | ||
<StructureSection load='2m8c' size='340' side='right' caption='[[2m8c]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='2m8c' size='340' side='right' caption='[[2m8c]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[2m8c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M8C FirstGlance]. <br> | <table><tr><td colspan='2'>[[2m8c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M8C FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisJ, EcDH1_1347, ECDH1ME8569_2247 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisJ, EcDH1_1347, ECDH1ME8569_2247 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=536056 ECOD1])</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=2m8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8c OCA], [http://pdbe.org/2m8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m8c RCSB], [http://www.ebi.ac.uk/pdbsum/2m8c PDBsum]</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=2m8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8c OCA], [http://pdbe.org/2m8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m8c RCSB], [http://www.ebi.ac.uk/pdbsum/2m8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
Revision as of 02:04, 10 August 2018
The solution NMR structure of E. coli apo-HisJThe solution NMR structure of E. coli apo-HisJ
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMedEscherichia coli HisJ is a type II periplasmic binding protein (PBP) that functions to reversibly capture histidine and transfer it to its cognate inner membrane ABC permease. Here we used NMR spectroscopy to determine the structure of apo-HisJ (26.5 kDa) in solution. HisJ is a bilobal protein of which the domain 1 (D1) is made up of two non-contiguous subdomains and domain 2 (D2) is expressed as the inner domain. To better understand the roles of D1 and D2 we have isolated and characterized each domain separately. Structurally, D1 closely resembles its homologous domain in apo- and holo-HisJ, while D2 is more similar to the holo-form. NMR relaxation experiments reveal that HisJ becomes more ordered upon ligand binding, while isolated D2 experiences a significant reduction in slower (ms-mus) motions compared with the homologous domain in apo-HisJ. NMR titrations reveal that D1 is able to bind histidine in a similar manner as full-length HisJ, albeit with lower affinity. Unexpectedly, isolated D1 and D2 do not interact in the presence or absence of histidine, which indicates the importance of intact interdomain connecting elements (i.e. hinge regions) for HisJ functioning. Our results shed light on the binding mechanism of type II PBPs where ligand is initially bound by D1 and D2 plays a supporting role in this dynamic process. The Role of the Two Structural Domains from the Periplasmic E. coli Histidine Binding Protein HisJ.,Chu BC, Dewolf T, Vogel HJ J Biol Chem. 2013 Sep 13. PMID:24036119[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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