5hm4
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5hm4' size='340' side='right' caption='[[5hm4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5hm4' size='340' side='right' caption='[[5hm4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5hm4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HM4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hm4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HM4 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfu|4pfu]], [[4pfw|4pfw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfu|4pfu]], [[4pfw|4pfw]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tmari_1233 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=5hm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm4 OCA], [http://pdbe.org/5hm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hm4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm4 ProSAT]</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=5hm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm4 OCA], [http://pdbe.org/5hm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hm4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ligand-induced conformational changes of periplasmic binding proteins (PBP) play a key role in the acquisition of metabolites in ATP binding cassette (ABC) transport systems. This conformational change allows for differential recognition of the ligand occupancy of the PBP by the ABC transporter. This minimizes futile ATP hydrolysis in the transporter, a phenomenon in which ATP hydrolysis is not coupled to metabolite transport. In many systems, the PBP conformational change is insufficient at eliminating futile ATP hydrolysis. Here we identify an additional state of the PBP that is also allosterically regulated by the ligand. Ligand binding to the homodimeric apo PBP leads to a tightening of the interface alpha-helices so that the hydrogen bonding pattern shifts to that of a 310 helix, in-turn altering the contacts and the dynamics of the protein interface so that the monomer exists in the presence of ligand. | ||
| + | |||
| + | Periplasmic Binding Protein Dimer Has a Second Allosteric Event Tied to Ligand Binding.,Li L, Ghimire-Rijal S, Lucas SL, Stanley CB, Wright E, Agarwal PK, Myles DA, Cuneo MJ Biochemistry. 2017 Oct 10;56(40):5328-5337. doi: 10.1021/acs.biochem.7b00657., Epub 2017 Sep 22. PMID:28876049<ref>PMID:28876049</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5hm4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 43589]] | ||
[[Category: Cuneo, M J]] | [[Category: Cuneo, M J]] | ||
[[Category: Ghimire-Rijal, S]] | [[Category: Ghimire-Rijal, S]] | ||
Revision as of 08:21, 17 October 2018
Crystal structure of oligopeptide ABC transporter, periplasmic oligopeptide-binding protein (TM1226) from THERMOTOGA MARITIMA at 2.0 A resolution
| |||||||||||
