3th6: Difference between revisions

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<StructureSection load='3th6' size='340' side='right'caption='[[3th6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3th6' size='340' side='right'caption='[[3th6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3th6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Boophilus_microplus Boophilus microplus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TH6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3th6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhipicephalus_microplus Rhipicephalus microplus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TH6 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6941 Boophilus microplus])</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]] 2.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=3th6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3th6 OCA], [https://pdbe.org/3th6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3th6 RCSB], [https://www.ebi.ac.uk/pdbsum/3th6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3th6 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=3th6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3th6 OCA], [https://pdbe.org/3th6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3th6 RCSB], [https://www.ebi.ac.uk/pdbsum/3th6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3th6 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A8B3A8_RHIMP A8B3A8_RHIMP]
Triosephosphate isomerase (TIM) is an enzyme with a role in glycolysis and gluconeogenesis by catalyzing the interconversion between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. This enzyme has been used as a target in endoparasite drug development. In this work we cloned, expressed, purified and studied kinetic and structural characteristics of TIM from tick embryos, Rhipicephalus (Boophilus) microplus (BmTIM). The Km and Vmax of the recombinant BmTIM with glyceraldehyde 3-phosphate as substrate, were 0.47 mM and 6031 mumol min(1) mg protein(1), respectively. The resolution of the diffracted crystal was estimated to be 2.4 A and the overall data showed that BmTIM is similar to other reported dimeric TIMs. However, we found that, in comparison to other TIMs, BmTIM has the highest content of cysteine residues (nine cysteine residues per monomer). Only two cysteines could make disulfide bonds in monomers of BmTIM. Furthermore, BmTIM was highly sensitive to the action of the thiol reagents dithionitrobenzoic acid and methyl methane thiosulfonate, suggesting that there are five cysteines exposed in each dimer and that these residues could be employed in the development of species-specific inhibitors.
 
Structural and biochemical characterization of a recombinant triosephosphate isomerase from Rhipicephalus (Boophilus) microplus.,Moraes J, Arreola R, Cabrera N, Saramago L, Freitas D, Masuda A, da Silva Vaz I Jr, Tuena de Gomez-Puyou M, Perez-Montfort R, Gomez-Puyou A, Logullo C Insect Biochem Mol Biol. 2011 Jun;41(6):400-9. Epub 2011 Mar 9. PMID:21396445<ref>PMID:21396445</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3th6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Boophilus microplus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Triose-phosphate isomerase]]
[[Category: Rhipicephalus microplus]]
[[Category: Arreola, R]]
[[Category: Arreola R]]
[[Category: Gomez-Puyou, A]]
[[Category: Gomez-Puyou A]]
[[Category: Logullo, C]]
[[Category: Logullo C]]
[[Category: Moraes, J]]
[[Category: Moraes J]]
[[Category: Perez-Montfort, R]]
[[Category: Perez-Montfort R]]
[[Category: Rodriguez-Romero, A]]
[[Category: Rodriguez-Romero A]]
[[Category: Alpha/beta barrel]]
[[Category: Embryogenesis]]
[[Category: Glycolysis]]
[[Category: Isomerase]]

Latest revision as of 13:28, 14 March 2024

Crystal structure of Triosephosphate isomerase from Rhipicephalus (Boophilus) microplus.

3th6, resolution 2.40Å

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