1njr: Difference between revisions

Revision as of 15:06, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1NJR is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:06:49 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1njr.gif|left|200px]]<br /><applet load="1njr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1njr.gif|left|200px]]<br /><applet load="1njr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1njr, resolution 1.9&Aring;" />
 '''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase'''<br />
 ==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==
-NJR 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 XYL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NJR OCA].
+NJR 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=XYL:'>XYL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJR OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Burley, S.K.]]
+[[Category: Burley, S K.]]
 [[Category: Eswaramoorthy, S.]]
 [[Category: Kumaran, D.]]
-[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
+[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
-[[Category: Studier, F.W.]]
+[[Category: Studier, F W.]]
 [[Category: Swaminathan, S.]]
 [[Category: XYL]]
@@ Line 28: / Line 28: @@
 [[Category: two domain organization]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:19:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:49 2008''