1o2b

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|PDB= 1o2b |SIZE=350|CAPTION= <scene name='initialview01'>1o2b</scene>, resolution 2.45&Aring;
|PDB= 1o2b |SIZE=350|CAPTION= <scene name='initialview01'>1o2b</scene>, resolution 2.45&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= TM0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
|GENE= TM0449 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
 +
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00847 thyX]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o2b OCA], [http://www.ebi.ac.uk/pdbsum/1o2b PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1o2b RCSB]</span>
}}
}}
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[[Category: Mathews, I I.]]
[[Category: Mathews, I I.]]
[[Category: McMullan, D.]]
[[Category: McMullan, D.]]
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[[Category: FAD]]
 
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[[Category: PO4]]
 
[[Category: jcsg]]
[[Category: jcsg]]
[[Category: joint center for structural genomic]]
[[Category: joint center for structural genomic]]
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[[Category: tm0449]]
[[Category: tm0449]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:04:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 25 23:24:58 2008''

Revision as of 21:24, 25 March 2008


PDB ID 1o2b

Drag the structure with the mouse to rotate
, resolution 2.45Å
Ligands: ,
Gene: TM0449 (Thermotoga maritima)
Domains: thyX
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and PO4 at 2.45 A resolution


Overview

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.

About this Structure

1O2B is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

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

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