View source for 5anp


==CRYSTAL STRUCTURE OF THE BA41 PROTEIN FROM BIZIONIA ARGENTINENSIS==
<StructureSection load='5anp' size='340' side='right'caption='[[5anp]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5anp]] is a 2 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=5ANP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ANP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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=5anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5anp OCA], [https://pdbe.org/5anp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5anp RCSB], [https://www.ebi.ac.uk/pdbsum/5anp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5anp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G2EA44_9FLAO G2EA44_9FLAO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Pfam PF04536 TPM_phosphatase family is a broadly conserved family of domains found across prokaryotes, plants and invertebrates. Despite having a similar protein fold, members of this family have been implicated in diverse cellular processes and found in varied subcellular localizations. Very recently, the biochemical characterization of two evolutionary divergent TPM domains has shown that they are able to hydrolyze phosphate groups from different substrates. However, there are still incorrect functional annotations and uncertain relationships between the structure and function of this family of domains. BA41 is an uncharacterized single-pass transmembrane protein from the Antarctic psychrotolerant bacterium Bizionia argentinensis with a predicted compact extracytoplasmic TPM domain and a C-terminal cytoplasmic low complexity region. To shed light on the structural properties that enable TPM domains to adopt divergent roles, we here accomplish a comprehensive structural and functional characterization of the central TPM domain of BA41 (BA41-TPM). Contrary to its predicted function as a beta-propeller methanol dehydrogenase, light scattering and crystallographic studies showed that BA41-TPM behaves as a globular monomeric protein and adopts a conserved Rossmann fold, typically observed in other TPM domain structures. Although the crystal structure reveals the conservation of residues involved in substrate binding, no putative catalytic or intramolecular metal ions were detected. Most important, however, extensive biochemical studies demonstrated that BA41-TPM has hydrolase activity against ADP, ATP, and other di- and triphosphate nucleotides and shares properties of cold-adapted enzymes. The role of BA41 in extracellular ATP-mediated signaling pathways and its occurrence in environmental and pathogenic microorganisms is discussed.

Structural and functional characterization of a cold adapted TPM-domain with ATPase/ADPase activity.,Cerutti ML, Otero LH, Smal C, Pellizza L, Goldbaum FA, Klinke S, Aran M J Struct Biol. 2016 Nov 1. pii: S1047-8477(16)30230-1. doi:, 10.1016/j.jsb.2016.10.010. PMID:27810564<ref>PMID:27810564</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5anp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bizionia argentinensis JUB59]]
[[Category: Large Structures]]
[[Category: Cerutti ML]]
[[Category: Goldbaum FA]]
[[Category: Klinke S]]
[[Category: Otero LH]]