View source for 4oa3


==Crystal structure of the BA42 protein from BIZIONIA ARGENTINENSIS==
<StructureSection load='4oa3' size='340' side='right'caption='[[4oa3]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4oa3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lt2|2lt2]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BZARG_1551 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1046627 Bizionia argentinensis JUB59])</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=4oa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oa3 OCA], [http://pdbe.org/4oa3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oa3 RCSB], [http://www.ebi.ac.uk/pdbsum/4oa3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oa3 ProSAT]</span></td></tr>
</table>
<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 4oa3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acid phosphatase|Acid phosphatase]]
*[[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: Goldbaum, F A]]
[[Category: Klinke, S]]
[[Category: Otero, L H]]
[[Category: Pellizza, L]]
[[Category: Ba42]]
[[Category: Unknown function]]