This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3s86

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:48, 1 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3s86' size='340' side='right'caption='[[3s86]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3s86' size='340' side='right'caption='[[3s86]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3s86]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S86 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3s86]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S86 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vp2|1vp2]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0159 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nucleoside-triphosphatase Nucleoside-triphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.15 3.6.1.15] </span></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=3s86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s86 OCA], [https://pdbe.org/3s86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s86 RCSB], [https://www.ebi.ac.uk/pdbsum/3s86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s86 ProSAT]</span></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=3s86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s86 OCA], [https://pdbe.org/3s86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s86 RCSB], [https://www.ebi.ac.uk/pdbsum/3s86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s86 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/NTPA_THEMA NTPA_THEMA]] Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP/dITP to their respective monophosphate derivatives. Might exclude non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions.[HAMAP-Rule:MF_01405]
+
[https://www.uniprot.org/uniprot/IXTPA_THEMA IXTPA_THEMA] Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.[HAMAP-Rule:MF_01405]
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The hyperthermophilic bacterium Thermotoga maritima has a noncanonical nucleoside triphosphatase that catalyzes the conversion of inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) into inosine monophosphate (IMP), deoxyinosine monophosphate (IMP) and xanthosine monophosphate (XMP), respectively. The k(cat)/K(m) values determined at 323 and 353 K fall between 1.31 x 10(4) and 7.80 x 10(4) M(-1) s(-1). ITP and dITP are slightly preferred over XTP. Activity towards canonical nucleoside triphosphates (ATP and GTP) was not detected. The enzyme has an absolute requirement for Mg(2+) as a cofactor and has a preference for alkaline conditions. A protein X-ray structure of the enzyme with bound IMP was obtained at 2.15 A resolution. The active site houses a well conserved network of residues that are critical for substrate recognition and catalysis. The crystal structure shows a tetramer with two possible dimer interfaces. One of these interfaces strongly resembles the dimer interface that is found in the structures of other noncanonical nucleoside pyrophosphatases from human (human ITPase) and archaea (Mj0226 and PhNTPase).
+
-
 
+
-
Structural and functional characterization of a noncanonical nucleoside triphosphate pyrophosphatase from Thermotoga maritima.,Awwad K, Desai A, Smith C, Sommerhalter M Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):184-93. doi:, 10.1107/S0907444912044630. Epub 2013 Jan 18. PMID:23385455<ref>PMID:23385455</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3s86" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Nucleoside triphosphatase|Nucleoside triphosphatase]]
*[[Nucleoside triphosphatase|Nucleoside triphosphatase]]
*[[Sandbox 30008|Sandbox 30008]]
*[[Sandbox 30008|Sandbox 30008]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Nucleoside-triphosphatase]]
+
[[Category: Thermotoga maritima]]
-
[[Category: Awwad, K]]
+
[[Category: Awwad K]]
-
[[Category: Desai, A]]
+
[[Category: Desai A]]
-
[[Category: Smith, C]]
+
[[Category: Smith C]]
-
[[Category: Sommerhalter, M]]
+
[[Category: Sommerhalter M]]
-
[[Category: Hydrolase]]
+
-
[[Category: Long twisted beta strand covered by two lobe]]
+
-
[[Category: Non-canonical nucleoside triphosphatase]]
+

Current revision

Crystal Structure of TM0159 with bound IMP

PDB ID 3s86

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3s86"
Personal tools