9gaa: Difference between revisions

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New page: left|200px<br /><applet load="9gaa" size="450" color="white" frame="true" align="right" spinBox="true" caption="9gaa, resolution 2.1Å" /> '''PRECURSOR OF THE T152...
 
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[[Image:9gaa.gif|left|200px]]<br /><applet load="9gaa" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:9gaa.gif|left|200px]]<br /><applet load="9gaa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="9gaa, resolution 2.1&Aring;" />
caption="9gaa, resolution 2.1&Aring;" />
'''PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''<br />
'''PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''<br />


==Overview==
==Overview==
A variety of proteins, including glycosylasparaginase, have recently been, found to activate functions by self-catalyzed peptide bond rearrangements, from single-chain precursors. Here we present the 1.9 A crystal structures, of glycosylasparaginase precursors that are able to autoproteolyze via an, N --&gt; O acyl shift. Several conserved residues are aligned around the, scissile peptide bond that is in a highly strained trans peptide bond, configuration. The structure illustrates how a nucleophilic side chain may, attack the scissile peptide bond at the immediate upstream backbone, carbonyl and provides an understanding of the structural basis for peptide, bond cleavage via an N --&gt; O or N --&gt; S acyl shift that is used by various, groups of intramolecular autoprocessing proteins.
A variety of proteins, including glycosylasparaginase, have recently been found to activate functions by self-catalyzed peptide bond rearrangements from single-chain precursors. Here we present the 1.9 A crystal structures of glycosylasparaginase precursors that are able to autoproteolyze via an N --&gt; O acyl shift. Several conserved residues are aligned around the scissile peptide bond that is in a highly strained trans peptide bond configuration. The structure illustrates how a nucleophilic side chain may attack the scissile peptide bond at the immediate upstream backbone carbonyl and provides an understanding of the structural basis for peptide bond cleavage via an N --&gt; O or N --&gt; S acyl shift that is used by various groups of intramolecular autoprocessing proteins.


==About this Structure==
==About this Structure==
9GAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Active as [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=9GAA OCA].  
9GAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Active as [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GAA OCA].  


==Reference==
==Reference==
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[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Guo, H.C.]]
[[Category: Guo, H C.]]
[[Category: Xu, Q.]]
[[Category: Xu, Q.]]
[[Category: autoproteolysis]]
[[Category: autoproteolysis]]
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[[Category: precursor]]
[[Category: precursor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:02:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:30 2008''

Revision as of 20:18, 21 February 2008

File:9gaa.gif


9gaa, resolution 2.1Å

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PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

OverviewOverview

A variety of proteins, including glycosylasparaginase, have recently been found to activate functions by self-catalyzed peptide bond rearrangements from single-chain precursors. Here we present the 1.9 A crystal structures of glycosylasparaginase precursors that are able to autoproteolyze via an N --> O acyl shift. Several conserved residues are aligned around the scissile peptide bond that is in a highly strained trans peptide bond configuration. The structure illustrates how a nucleophilic side chain may attack the scissile peptide bond at the immediate upstream backbone carbonyl and provides an understanding of the structural basis for peptide bond cleavage via an N --> O or N --> S acyl shift that is used by various groups of intramolecular autoprocessing proteins.

About this StructureAbout this Structure

9GAA is a Single protein structure of sequence from Elizabethkingia meningoseptica. Active as N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into the mechanism of intramolecular proteolysis., Xu Q, Buckley D, Guan C, Guo HC, Cell. 1999 Sep 3;98(5):651-61. PMID:10490104

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