1o27: Difference between revisions
New page: left|200px<br /><applet load="1o27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o27, resolution 2.3Å" /> '''Crystal structure of ... |
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[[Image:1o27.gif|left|200px]]<br /><applet load="1o27" size=" | [[Image:1o27.gif|left|200px]]<br /><applet load="1o27" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1o27, resolution 2.3Å" /> | caption="1o27, resolution 2.3Å" /> | ||
'''Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and BrdUMP at 2.3 A resolution'''<br /> | '''Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and BrdUMP at 2.3 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
Like thymidylate synthase (TS) in eukaryotes, the thymidylate | 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== | ==About this Structure== | ||
1O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with FAD and BRU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=BRU:'>BRU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O27 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Agarwalla, S.]] | [[Category: Agarwalla, S.]] | ||
[[Category: Canaves, J | [[Category: Canaves, J M.]] | ||
[[Category: Deacon, A | [[Category: Deacon, A M.]] | ||
[[Category: JCSG, Joint | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
[[Category: Kuhn, P.]] | [[Category: Kuhn, P.]] | ||
[[Category: Lesley, S | [[Category: Lesley, S A.]] | ||
[[Category: Mathews, I | [[Category: Mathews, I I.]] | ||
[[Category: McMullan, D.]] | [[Category: McMullan, D.]] | ||
[[Category: BRU]] | [[Category: BRU]] | ||
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[[Category: tm0449]] | [[Category: tm0449]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:31 2008'' | ||
Revision as of 15:12, 21 February 2008
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Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and BrdUMP at 2.3 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
1O27 is a Single protein structure of sequence from Thermotoga maritima with and as ligands. 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
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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.
- BRU
- FAD
- Jcsg
- Joint center for structural genomics
- Protein structure initiative
- Psi
- Structural genomics
- Thymidylate synthase complementing protein
- Tm0449