4y23: Difference between revisions
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''' | ==Crystal structure of T399A precursor mutant protein of gamma-glutamyl transpeptidase from Bacillus licheniformis== | ||
<StructureSection load='4y23' size='340' side='right' caption='[[4y23]], [[Resolution|resolution]] 2.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4y23]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y23 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eow|2eow]], [[4ott|4ott]], [[4otu|4otu]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y23 OCA], [http://pdbe.org/4y23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y23 RCSB], [http://www.ebi.ac.uk/pdbsum/4y23 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
gamma-Glutamyl transpeptidases (gamma-GTs) are members of N-terminal nucleophile hydrolase superfamily. They are synthetized as single-chain precursors, which are then cleaved to form mature enzymes. Basic aspects of autocatalytic processing of these pro-enzymes are still unknown. Here we describe the X-ray structure of the precursor mimic of Bacillus licheniformis gamma-GT (BlGT), obtained by mutating catalytically important threonine to alanine (T399A-BlGT), and report results of autoprocessing of mutants of His401, Thr415, Thr417, Glu419 and Arg571. Data suggest that Thr417 is in a competent position to activate the catalytic threonine (Thr399) for nucleophilic attack of the scissile peptide bond and that Thr415 plays a major role in assisting the process. On the basis of these new structural results, a possible mechanism of autoprocessing is proposed. This mechanism, which guesses the existence of a six-membered transition state involving one carbonyl and two hydroxyl groups, is in agreement with all the available experimental data collected on gamma-GTs from different species and with our new Ala-scanning mutagenesis data. | |||
The | The maturation mechanism of gamma-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies.,Pica A, Chi MC, Chen YY, d'Ischia M, Lin LL, Merlino A Biochim Biophys Acta. 2015 Oct 30. pii: S1570-9639(15)00268-X. doi:, 10.1016/j.bbapap.2015.10.006. PMID:26536828<ref>PMID:26536828</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4y23" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Merlino, A]] | [[Category: Merlino, A]] | ||
[[Category: Pica, A]] | [[Category: Pica, A]] | ||
[[Category: Gamma-gtp]] | |||
[[Category: Maturation]] | |||
[[Category: Ntn hydrolase]] | |||
[[Category: Post-translational processing]] | |||
[[Category: Precursor]] | |||
[[Category: Transferase]] | |||
Revision as of 18:57, 1 December 2015
Crystal structure of T399A precursor mutant protein of gamma-glutamyl transpeptidase from Bacillus licheniformis
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