View source for 2mpb


==NMR structure of BA42 protein from the psychrophilic bacteria Bizionia argentinensis sp. nov==
<StructureSection load='2mpb' size='340' side='right'caption='[[2mpb]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mpb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bizionia_argentinensis_JUB59 Bizionia argentinensis JUB59]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpb OCA], [https://pdbe.org/2mpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mpb RCSB], [https://www.ebi.ac.uk/pdbsum/2mpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G2EA45_9FLAO G2EA45_9FLAO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:25116514</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mpb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
*[[BA42|BA42]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bizionia argentinensis JUB59]]
[[Category: Large Structures]]
[[Category: Aran M]]
[[Category: Cicero D]]
[[Category: Gallo M]]
[[Category: Pellizza L]]
[[Category: Smal C]]