1o2a: Difference between revisions
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|PDB= 1o2a |SIZE=350|CAPTION= <scene name='initialview01'>1o2a</scene>, resolution 1.8Å | |PDB= 1o2a |SIZE=350|CAPTION= <scene name='initialview01'>1o2a</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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> | |||
|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.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1o2a RCSB]</span> | |||
}} | }} | ||
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[[Category: Mathews, I I.]] | [[Category: Mathews, I I.]] | ||
[[Category: McMullan, D.]] | [[Category: McMullan, D.]] | ||
[[Category: jcsg]] | [[Category: jcsg]] | ||
[[Category: joint center for structural genomic]] | [[Category: joint center for structural genomic]] | ||
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[[Category: tm0449]] | [[Category: tm0449]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 25 23:24:57 2008'' | ||
Revision as of 00:24, 26 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 at 1.8 A resolution
OverviewOverview
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 StructureAbout this Structure
1O2A is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Tue Mar 25 23:24:57 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Single protein
- Thermotoga maritima
- Agarwalla, S.
- Canaves, J M.
- Deacon, A M.
- JCSG, Joint Center for Structural Genomics.
- Kuhn, P.
- Lesley, S A.
- Mathews, I I.
- McMullan, D.
- Jcsg
- Joint center for structural genomic
- Protein structure initiative
- Psi
- Structural genomic
- Thymidylate synthase complementing protein
- Tm0449