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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[[Image:1o2a.jpg|left|200px]]<br /><applet load="1o2a" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1o2a.jpg|left|200px]]<br /><applet load="1o2a" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1o2a, resolution 1.8&Aring;" />
caption="1o2a, resolution 1.8&Aring;" />
'''Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution'''<br />
'''Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD at 1.8 A resolution'''<br />


==Overview==
==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.
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==
1O2A 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O2A OCA].  
1O2A 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O2A OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Agarwalla, S.]]
[[Category: Agarwalla, S.]]
[[Category: Canaves, J.M.]]
[[Category: Canaves, J M.]]
[[Category: Deacon, A.M.]]
[[Category: Deacon, A M.]]
[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
[[Category: Lesley, S.A.]]
[[Category: Lesley, S A.]]
[[Category: Mathews, I.I.]]
[[Category: Mathews, I I.]]
[[Category: McMullan, D.]]
[[Category: McMullan, D.]]
[[Category: FAD]]
[[Category: FAD]]
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[[Category: tm0449]]
[[Category: tm0449]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:45:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:33 2008''

Revision as of 15:12, 21 February 2008

File:1o2a.jpg


1o2a, resolution 1.8Å

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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 with as ligand. 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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