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[[Image:1o2a.jpg|left|200px]]


{{Structure
==Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution==
|PDB= 1o2a |SIZE=350|CAPTION= <scene name='initialview01'>1o2a</scene>, resolution 1.8&Aring;
<StructureSection load='1o2a' size='340' side='right'caption='[[1o2a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
<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>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE= TM0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
<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>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00847 thyX]</span>
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o2a OCA], [http://www.ebi.ac.uk/pdbsum/1o2a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o2a RCSB]</span>
== 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.


'''Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1o2a" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1O2A is a [[Single protein]] structure of sequence from [http://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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12791256 12791256]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Agarwalla, S.]]
[[Category: Agarwalla S]]
[[Category: Canaves, J M.]]
[[Category: Canaves JM]]
[[Category: Deacon, A M.]]
[[Category: Deacon AM]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: Kuhn P]]
[[Category: Kuhn, P.]]
[[Category: Lesley SA]]
[[Category: Lesley, S A.]]
[[Category: Mathews II]]
[[Category: Mathews, I I.]]
[[Category: McMullan D]]
[[Category: McMullan, D.]]
[[Category: jcsg]]
[[Category: joint center for structural genomic]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomic]]
[[Category: thymidylate synthase complementing protein]]
[[Category: tm0449]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:38:47 2008''

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

1o2a is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THYX_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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Mathews II, Deacon AM, Canaves JM, McMullan D, Lesley SA, Agarwalla S, Kuhn P. Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein. Structure. 2003 Jun;11(6):677-90. PMID:12791256

1o2a, resolution 1.80Å

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