1o26: Difference between revisions
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<StructureSection load='1o26' size='340' side='right'caption='[[1o26]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1o26' size='340' side='right'caption='[[1o26]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1o26]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1o26]] 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=1O26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O26 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</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=1o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o26 OCA], [https://pdbe.org/1o26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o26 RCSB], [https://www.ebi.ac.uk/pdbsum/1o26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o26 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 37: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Agarwalla S]] | ||
[[Category: | [[Category: Canaves JM]] | ||
[[Category: | [[Category: Deacon AM]] | ||
[[Category: Kuhn | [[Category: Kuhn P]] | ||
[[Category: Lesley | [[Category: Lesley SA]] | ||
[[Category: Mathews | [[Category: Mathews II]] | ||
[[Category: McMullan | [[Category: McMullan D]] | ||
Latest revision as of 17:51, 20 September 2023
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and dUMP at 1.6 A resolutionCrystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and dUMP at 1.6 A resolution
Structural highlights
FunctionTHYX_THEMA Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLike thymidylate synthase (TS) in eukaryotes, the thymidylate synthase-complementing proteins (TSCPs) are mandatory for cell survival of many prokaryotes in the absence of external sources of thymidylate. Details of the mechanism of this novel family of enzymes are unknown. Here, we report the structural and functional analysis of a TSCP from Thermotoga maritima and its complexes with substrate, analogs, and cofactor. The structures presented here provide a basis for rationalizing the TSCP catalysis and reveal the possibility of the design of an inhibitor. We have identified a new helix-loop-strand FAD binding motif characteristic of the enzymes in the TSCP family. The presence of a hydrophobic core with residues conserved among the TSCP family suggests a common overall fold. Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein.,Mathews II, Deacon AM, Canaves JM, McMullan D, Lesley SA, Agarwalla S, Kuhn P Structure. 2003 Jun;11(6):677-90. PMID:12791256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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