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4rwx

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<StructureSection load='4rwx' size='340' side='right'caption='[[4rwx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='4rwx' size='340' side='right'caption='[[4rwx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rwx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rwx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RWX FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rww|4rww]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmo2692 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwx OCA], [https://pdbe.org/4rwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rwx RCSB], [https://www.ebi.ac.uk/pdbsum/4rwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwx ProSAT]</span></td></tr>
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<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=4rwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwx OCA], [http://pdbe.org/4rwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwx RCSB], [http://www.ebi.ac.uk/pdbsum/4rwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwx ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8Y3Y7_LISMO Q8Y3Y7_LISMO]
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Cyclic-di-AMP (c-di-AMP) is a broadly conserved bacterial second messenger that is of importance in bacterial physiology. The molecular receptors mediating the cellular responses to the c-di-AMP signal are just beginning to be discovered. PstA is a previously uncharacterized PII -like protein which has been identified as a c-di-AMP receptor. PstA is widely distributed and conserved among Gram-positive bacteria in the phylum Firmicutes. Here, we report the biochemical, structural, and functional characterization of PstA from Listeria monocytogenes. We have determined the crystal structures of PstA in the c-di-AMP-bound and apo forms at 1.6 and 2.9 A resolution, respectively, which provide the molecular basis for its specific recognition of c-di-AMP. PstA forms a homotrimer structure that has overall similarity to the PII protein family which binds ATP. However, PstA is markedly different from PII proteins in the loop regions, and these structural differences mediate the specific recognition of their respective nucleotide ligand. The residues composing the c-di-AMP binding pocket are conserved, suggesting that c-di-AMP recognition by PstA is of functional importance. Disruption of pstA in L. monocytogenes affected c-di-AMP-mediated alterations in bacterial growth and lysis. Overall, we have defined the PstA family as a conserved and specific c-di-AMP receptor in bacteria.
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Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII -like signal transduction protein.,Choi PH, Sureka K, Woodward JJ, Tong L Microbiologyopen. 2015 Jun;4(3):361-74. doi: 10.1002/mbo3.243. Epub 2015 Feb 18. PMID:25693966<ref>PMID:25693966</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4rwx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lismo]]
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[[Category: Listeria monocytogenes EGD-e]]
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[[Category: Choi, P H]]
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[[Category: Choi PH]]
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[[Category: Tong, L]]
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[[Category: Tong L]]
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[[Category: Pii-like]]
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[[Category: Protein binding]]
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Current revision

Crystal Structure of L. monocytogenes PstA

PDB ID 4rwx

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