4oa3: Difference between revisions
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<StructureSection load='4oa3' size='340' side='right'caption='[[4oa3]], [[Resolution|resolution]] 1.39Å' scene=''> | <StructureSection load='4oa3' size='340' side='right'caption='[[4oa3]], [[Resolution|resolution]] 1.39Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4oa3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4oa3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bizionia_argentinensis_JUB59 Bizionia argentinensis JUB59]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OA3 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><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4oa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oa3 OCA], [https://pdbe.org/4oa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oa3 RCSB], [https://www.ebi.ac.uk/pdbsum/4oa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oa3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G2EA45_9FLAO G2EA45_9FLAO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bizionia argentinensis | [[Category: Bizionia argentinensis JUB59]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aran | [[Category: Aran M]] | ||
[[Category: Cicero | [[Category: Cicero D]] | ||
[[Category: Goldbaum | [[Category: Goldbaum FA]] | ||
[[Category: Klinke | [[Category: Klinke S]] | ||
[[Category: Otero | [[Category: Otero LH]] | ||
[[Category: Pellizza | [[Category: Pellizza L]] | ||
Revision as of 10:13, 25 January 2023
Crystal structure of the BA42 protein from BIZIONIA ARGENTINENSISCrystal structure of the BA42 protein from BIZIONIA ARGENTINENSIS
Structural highlights
FunctionPublication Abstract from PubMedThe structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by Nuclear Magnetic Resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four beta-strands constituting the central beta-sheet of the alphabetaalpha architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain.,Aran M, Smal C, Pellizza L, Gallo M, Otero LH, Klinke S, Goldbaum FA, Ithurralde ER, Bercovich A, Mac Cormack WP, Turjanski AG, Cicero DO Proteins. 2014 Aug 13. doi: 10.1002/prot.24667. PMID:25116514[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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