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New page: left|200px<br /><applet load="1txz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1txz, resolution 2.05Å" /> '''Crystal structure of...
 
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[[Image:1txz.jpg|left|200px]]<br /><applet load="1txz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1txz.jpg|left|200px]]<br /><applet load="1txz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1txz, resolution 2.05&Aring;" />
caption="1txz, resolution 2.05&Aring;" />
'''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase, complexed with ADP-ribose'''<br />
'''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase, complexed with ADP-ribose'''<br />


==Overview==
==Overview==
Appr-1''-pase, an important and ubiquitous cellular processing enzyme, involved in the tRNA splicing pathway, catalyzes the conversion of, ADP-ribose-1''monophosphate (Appr-1''-p) to ADP-ribose. The structures of, the native enzyme from the yeast and its complex with ADP-ribose were, determined to 1.9 A and 2.05 A, respectively. Analysis of the, three-dimensional structure of this protein, selected as a target in a, structural genomics project, reveals its putative function and provides, clues to the catalytic mechanism. The structure of the 284-amino acid, protein shows a two-domain architecture consisting of a three-layer, alphabetaalpha sandwich N-terminal domain connected to a small C-terminal, helical domain. The structure of Appr-1''-pase in complex with the, product, ADP-ribose, reveals an active-site water molecule poised for, nucleophilic attack on the terminal phosphate group. Loop-region residues, Asn 80, Asp 90, and His 145 may form a catalytic triad.
Appr-1''-pase, an important and ubiquitous cellular processing enzyme involved in the tRNA splicing pathway, catalyzes the conversion of ADP-ribose-1''monophosphate (Appr-1''-p) to ADP-ribose. The structures of the native enzyme from the yeast and its complex with ADP-ribose were determined to 1.9 A and 2.05 A, respectively. Analysis of the three-dimensional structure of this protein, selected as a target in a structural genomics project, reveals its putative function and provides clues to the catalytic mechanism. The structure of the 284-amino acid protein shows a two-domain architecture consisting of a three-layer alphabetaalpha sandwich N-terminal domain connected to a small C-terminal helical domain. The structure of Appr-1''-pase in complex with the product, ADP-ribose, reveals an active-site water molecule poised for nucleophilic attack on the terminal phosphate group. Loop-region residues Asn 80, Asp 90, and His 145 may form a catalytic triad.


==About this Structure==
==About this Structure==
1TXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4, NA, APR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TXZ OCA].  
1TXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=APR:'>APR</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXZ OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Burley, S.K.]]
[[Category: Burley, S K.]]
[[Category: Kumaran, D.]]
[[Category: Kumaran, D.]]
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
[[Category: APR]]
[[Category: APR]]
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[[Category: two domain organization]]
[[Category: two domain organization]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:31 2008''

Revision as of 13:18, 21 February 2008

File:1txz.jpg


1txz, resolution 2.05Å

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Crystal structure of yeast ymx7, an ADP-ribose-1-monophosphatase, complexed with ADP-ribose

Overview

Appr-1-pase, an important and ubiquitous cellular processing enzyme involved in the tRNA splicing pathway, catalyzes the conversion of ADP-ribose-1monophosphate (Appr-1-p) to ADP-ribose. The structures of the native enzyme from the yeast and its complex with ADP-ribose were determined to 1.9 A and 2.05 A, respectively. Analysis of the three-dimensional structure of this protein, selected as a target in a structural genomics project, reveals its putative function and provides clues to the catalytic mechanism. The structure of the 284-amino acid protein shows a two-domain architecture consisting of a three-layer alphabetaalpha sandwich N-terminal domain connected to a small C-terminal helical domain. The structure of Appr-1-pase in complex with the product, ADP-ribose, reveals an active-site water molecule poised for nucleophilic attack on the terminal phosphate group. Loop-region residues Asn 80, Asp 90, and His 145 may form a catalytic triad.

About this Structure

1TXZ is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4, NA, APR and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of ADP-ribose-1-monophosphatase (Appr-1-pase), a ubiquitous cellular processing enzyme., Kumaran D, Eswaramoorthy S, Studier FW, Swaminathan S, Protein Sci. 2005 Mar;14(3):719-26. PMID:15722447

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