1qcq

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(New page: 200px<br /><applet load="1qcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qcq, resolution 2.7&Aring;" /> '''UBIQUITIN CONJUGATING...)
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[[Image:1qcq.gif|left|200px]]<br /><applet load="1qcq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qcq, resolution 2.7&Aring;" />
caption="1qcq, resolution 2.7&Aring;" />
'''UBIQUITIN CONJUGATING ENZYME'''<br />
'''UBIQUITIN CONJUGATING ENZYME'''<br />
==Overview==
==Overview==
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The three-dimensional structure of a yeast ubiquitin-conjugating enzyme, encoded by the Saccharomyces cerevisiae UBC4 gene, has been determined at, 2.7 A. The structure was solved using molecular replacement techniques and, refined by simulated annealing to an R-factor of 0.198. Bond lengths and, angles in the molecule have root mean square deviations from ideal values, of 0.018 A and 4.0 degrees, respectively. Ubc4 is an alpha/beta protein, with four alpha-helices and a four-stranded antiparallel beta-sheet. The, ubiquitin-accepting cysteine is located in a cleft between two loops., Comparison with the recently determined structure of a different plant, enzyme suggests that class I ubiquitin-conjugating enzymes are highly, conserved in their three-dimensional folding. Except for two extra, residues at the N- and the C-terminus of the plant enzyme, the C alpha, atoms of the two enzymes can be superimposed with a root mean square, deviation of only 1.52 A. Greater variations are found between the, surfaces of the two molecules, as most of the identical residues between, the two enzymes are either buried or clustered on the surface that lies, adjacent to the ubiquitin-accepting cysteine. We suggest that this, conserved surface functions in protein-protein binding during ubiquitin, thiol ester formation.
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The three-dimensional structure of a yeast ubiquitin-conjugating enzyme, encoded by the Saccharomyces cerevisiae UBC4 gene, has been determined at 2.7 A. The structure was solved using molecular replacement techniques and refined by simulated annealing to an R-factor of 0.198. Bond lengths and angles in the molecule have root mean square deviations from ideal values of 0.018 A and 4.0 degrees, respectively. Ubc4 is an alpha/beta protein with four alpha-helices and a four-stranded antiparallel beta-sheet. The ubiquitin-accepting cysteine is located in a cleft between two loops. Comparison with the recently determined structure of a different plant enzyme suggests that class I ubiquitin-conjugating enzymes are highly conserved in their three-dimensional folding. Except for two extra residues at the N- and the C-terminus of the plant enzyme, the C alpha atoms of the two enzymes can be superimposed with a root mean square deviation of only 1.52 A. Greater variations are found between the surfaces of the two molecules, as most of the identical residues between the two enzymes are either buried or clustered on the surface that lies adjacent to the ubiquitin-accepting cysteine. We suggest that this conserved surface functions in protein-protein binding during ubiquitin thiol ester formation.
==About this Structure==
==About this Structure==
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1QCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure superseeds the now removed PDB entry 2UCE. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QCQ OCA].
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1QCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry 2UCE. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QCQ OCA].
==Reference==
==Reference==
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[[Category: Ubiquitin--protein ligase]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Chau, V.]]
[[Category: Chau, V.]]
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[[Category: Cook, W.J.]]
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[[Category: Cook, W J.]]
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[[Category: Jeffrey, L.C.]]
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[[Category: Jeffrey, L C.]]
[[Category: Xu, Y.]]
[[Category: Xu, Y.]]
[[Category: ubiquitin]]
[[Category: ubiquitin]]
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[[Category: yeast]]
[[Category: yeast]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:34:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:16 2008''

Revision as of 12:38, 21 February 2008


1qcq, resolution 2.7Å

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UBIQUITIN CONJUGATING ENZYME

Overview

The three-dimensional structure of a yeast ubiquitin-conjugating enzyme, encoded by the Saccharomyces cerevisiae UBC4 gene, has been determined at 2.7 A. The structure was solved using molecular replacement techniques and refined by simulated annealing to an R-factor of 0.198. Bond lengths and angles in the molecule have root mean square deviations from ideal values of 0.018 A and 4.0 degrees, respectively. Ubc4 is an alpha/beta protein with four alpha-helices and a four-stranded antiparallel beta-sheet. The ubiquitin-accepting cysteine is located in a cleft between two loops. Comparison with the recently determined structure of a different plant enzyme suggests that class I ubiquitin-conjugating enzymes are highly conserved in their three-dimensional folding. Except for two extra residues at the N- and the C-terminus of the plant enzyme, the C alpha atoms of the two enzymes can be superimposed with a root mean square deviation of only 1.52 A. Greater variations are found between the surfaces of the two molecules, as most of the identical residues between the two enzymes are either buried or clustered on the surface that lies adjacent to the ubiquitin-accepting cysteine. We suggest that this conserved surface functions in protein-protein binding during ubiquitin thiol ester formation.

About this Structure

1QCQ is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 2UCE. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

Reference

Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4., Cook WJ, Jeffrey LC, Xu Y, Chau V, Biochemistry. 1993 Dec 21;32(50):13809-17. PMID:8268156

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