View source for 4ct8


==Competence or damage-inducible protein CinA from Thermus thermophilus==
<StructureSection load='4ct8' size='340' side='right'caption='[[4ct8]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ct8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CT8 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]] 2.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ct8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ct8 OCA], [https://pdbe.org/4ct8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ct8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ct8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ct8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SHB0_THET8 Q5SHB0_THET8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CinA is a widely distributed protein in Gram-positive and Gram-negative bacteria. It is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD. Here we report the determination of the crystal structure of CinA from Thermus thermophilus, in complex with several ligands. CinA was shown to have both nicotinamide mononucleotide (NMN) deamidase and ADP-ribose pyrophosphatase activities. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain; the C-terminal domain harbours the NMN deamidase activity and the structure of a complex with the product nicotinate mononucleotide suggests a mechanism for deamidation. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state. Structures of complexes with Mg2+/ADP-ribose, Mg2+/ATP and Mg2+/AMP suggest a mechanism for the ADP-ribose pyrophosphatase reaction which involves a rotation of the COG1058 domain dimer as part of the reaction cycle, so that each active site oscillates between open and closed forms, thus promoting catalysis.

Structure and Mechanism of the Bifunctional CinA Enzyme from Thermus thermophilus.,Karuppiah V, Thistlethwaite A, Dajani R, Warwicker J, Derrick JP J Biol Chem. 2014 Oct 13. pii: jbc.M114.608448. PMID:25313401<ref>PMID:25313401</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ct8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Derrick J]]
[[Category: Karuppiah V]]