9gaf: Difference between revisions

New page: left|200px<br /><applet load="9gaf" size="450" color="white" frame="true" align="right" spinBox="true" caption="9gaf, resolution 1.9Å" /> '''PRECURSOR OF THE W11F...
 
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[[Image:9gaf.gif|left|200px]]<br /><applet load="9gaf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:9gaf.gif|left|200px]]<br /><applet load="9gaf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="9gaf, resolution 1.9&Aring;" />
caption="9gaf, resolution 1.9&Aring;" />
'''PRECURSOR OF THE W11F MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''<br />
'''PRECURSOR OF THE W11F 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==
9GAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with GLY as [http://en.wikipedia.org/wiki/ligand ligand]. 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=9GAF OCA].  
9GAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with <scene name='pdbligand=GLY:'>GLY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=9GAF 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: GLY]]
[[Category: GLY]]
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[[Category: precursor]]
[[Category: precursor]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:30 2008''

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