1ym5: Difference between revisions

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New page: left|200px<br /><applet load="1ym5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ym5, resolution 2.05Å" /> '''Crystal structure of...
 
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[[Image:1ym5.gif|left|200px]]<br /><applet load="1ym5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ym5.gif|left|200px]]<br /><applet load="1ym5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ym5, resolution 2.05&Aring;" />
caption="1ym5, resolution 2.05&Aring;" />
'''Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily.'''<br />
'''Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily.'''<br />


==Overview==
==Overview==
In the Pseudomonas bacterial genomes, the PhzF proteins are involved in, the production of phenazine derivative antibiotic and antifungal, compounds. The PhzF superfamily however also encompasses proteins in all, genomes from bacteria to eukaryotes, for which no function has been, assigned. We have determined the three dimensional crystal structure at, 2.05 A resolution of YHI9, the yeast member of the PhzF family. YHI9 has a, fold similar to bacterial diaminopimelate epimerase, revealing a bimodular, structure with an internal symmetry. Residue conservation identifies a, putative active site at the interface between the two domains. Evolution, of this protein by gene duplication, gene fusion and domain swapping from, an ancestral gene containing the "hot dog" fold, identifies the protein as, a "kinked double hot dog" fold.
In the Pseudomonas bacterial genomes, the PhzF proteins are involved in the production of phenazine derivative antibiotic and antifungal compounds. The PhzF superfamily however also encompasses proteins in all genomes from bacteria to eukaryotes, for which no function has been assigned. We have determined the three dimensional crystal structure at 2.05 A resolution of YHI9, the yeast member of the PhzF family. YHI9 has a fold similar to bacterial diaminopimelate epimerase, revealing a bimodular structure with an internal symmetry. Residue conservation identifies a putative active site at the interface between the two domains. Evolution of this protein by gene duplication, gene fusion and domain swapping from an ancestral gene containing the "hot dog" fold, identifies the protein as a "kinked double hot dog" fold.


==About this Structure==
==About this Structure==
1YM5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YM5 OCA].  
1YM5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YM5 OCA].  


==Reference==
==Reference==
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[[Category: Quevillon-Cheruel, S.]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Sorel, I.]]
[[Category: Sorel, I.]]
[[Category: Tilbeurgh, H.Van.]]
[[Category: Tilbeurgh, H Van.]]
[[Category: YSG, Paris-Sud.Yeast.Structural.Genomics.]]
[[Category: YSG, Paris-Sud Yeast Structural Genomics.]]
[[Category: double hot-dog]]
[[Category: double hot-dog]]
[[Category: paris-sud yeast structural genomics]]
[[Category: paris-sud yeast structural genomics]]
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[[Category: ysg]]
[[Category: ysg]]


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Revision as of 17:06, 21 February 2008

File:1ym5.gif


1ym5, resolution 2.05Å

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Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily.

OverviewOverview

In the Pseudomonas bacterial genomes, the PhzF proteins are involved in the production of phenazine derivative antibiotic and antifungal compounds. The PhzF superfamily however also encompasses proteins in all genomes from bacteria to eukaryotes, for which no function has been assigned. We have determined the three dimensional crystal structure at 2.05 A resolution of YHI9, the yeast member of the PhzF family. YHI9 has a fold similar to bacterial diaminopimelate epimerase, revealing a bimodular structure with an internal symmetry. Residue conservation identifies a putative active site at the interface between the two domains. Evolution of this protein by gene duplication, gene fusion and domain swapping from an ancestral gene containing the "hot dog" fold, identifies the protein as a "kinked double hot dog" fold.

About this StructureAbout this Structure

1YM5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily., Liger D, Quevillon-Cheruel S, Sorel I, Bremang M, Blondeau K, Aboulfath I, Janin J, van Tilbeurgh H, Leulliot N, Proteins. 2005 Sep 1;60(4):778-86. PMID:16021630

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