2dzy: Difference between revisions
New page: left|200px<br /><applet load="2dzy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dzy, resolution 2.57Å" /> '''Crystal structure of... |
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[[Image:2dzy.jpg|left|200px]]<br /><applet load="2dzy" size=" | [[Image:2dzy.jpg|left|200px]]<br /><applet load="2dzy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Crystal structure of N392A mutant of yeast bleomycin hydrolase'''<br /> | '''Crystal structure of N392A mutant of yeast bleomycin hydrolase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2DZY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] Full crystallographic information is available from [http:// | 2DZY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DZY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thiol protease]] | [[Category: thiol protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:09:36 2008'' | ||
Revision as of 15:09, 23 January 2008
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Crystal structure of N392A mutant of yeast bleomycin hydrolase
OverviewOverview
Bleomycin hydrolase (BH) is a hexameric papain family cysteine protease, which is involved in preparing peptides for antigen presentation and has, been implicated in tumour cell resistance to bleomycin chemotherapy., Structures of active-site mutants of yeast BH yielded unexpected results., Replacement of the active-site asparagine with alanine, valine or leucine, results in the destabilization of the histidine side chain, demonstrating, unambiguously the role of the asparagine residue in correctly positioning, the histidine for catalysis. Replacement of the histidine with alanine or, leucine destabilizes the asparagine position, indicating a delicate, arrangement of the active-site residues. In all of the mutants, the, C-terminus of the protein, which lies in the active site, protrudes, further into the active site. All mutants were compromised in their, catalytic activity. The structures also revealed the importance of a, tightly bound water molecule which stabilizes a loop near the active site, and which is conserved throughout the papain family. It is displaced in a, number of the mutants, causing destabilization of this loop and a nearby, loop, resulting in a large movement of the active-site cysteine. The, results imply that this water molecule plays a key structural role in this, family of enzymes.
About this StructureAbout this Structure
2DZY is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Bleomycin hydrolase, with EC number 3.4.22.40 Full crystallographic information is available from OCA.
ReferenceReference
Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure., O'Farrell PA, Joshua-Tor L, Biochem J. 2007 Jan 15;401(2):421-8. PMID:17007609
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