1o2a: Difference between revisions
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New page: left|200px<br /><applet load="1o2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o2a, resolution 1.8Å" /> '''Crystal structure of ... |
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== | ==Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution== | ||
Like thymidylate synthase (TS) in eukaryotes, the thymidylate | <StructureSection load='1o2a' size='340' side='right'caption='[[1o2a]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1o2a]] 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=1O2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O2A 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]] 1.8Å</td></tr> | |||
<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></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=1o2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o2a OCA], [https://pdbe.org/1o2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o2a RCSB], [https://www.ebi.ac.uk/pdbsum/1o2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o2a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o2/1o2a_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o2a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Like 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<ref>PMID:12791256</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: | <div class="pdbe-citations 1o2a" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Agarwalla | [[Category: Agarwalla S]] | ||
[[Category: Canaves | [[Category: Canaves JM]] | ||
[[Category: Deacon | [[Category: Deacon AM]] | ||
[[Category: Kuhn P]] | |||
[[Category: Kuhn | [[Category: Lesley SA]] | ||
[[Category: Lesley | [[Category: Mathews II]] | ||
[[Category: Mathews | [[Category: McMullan D]] | ||
[[Category: McMullan | |||
Latest revision as of 17:51, 20 September 2023
Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolutionCrystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 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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