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| | ==Crystal structure of T399A precursor mutant protein of gamma-glutamyl transpeptidase from Bacillus licheniformis== | | ==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=''> | + | <StructureSection load='4y23' size='340' side='right'caption='[[4y23]], [[Resolution|resolution]] 2.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y23]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. 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> | + | <table><tr><td colspan='2'>[[4y23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4y23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y23 OCA], [https://pdbe.org/4y23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y23 RCSB], [https://www.ebi.ac.uk/pdbsum/4y23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y23 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ggt, BL03798, BLi01364 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 "Clostridium licheniforme" Weigmann 1898])</td></tr>
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| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y23 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q65KZ6_BACLD Q65KZ6_BACLD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium licheniforme weigmann 1898]] | + | [[Category: Bacillus licheniformis]] |
| - | [[Category: Merlino, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Pica, A]] | + | [[Category: Merlino A]] |
| - | [[Category: Gamma-gtp]] | + | [[Category: Pica A]] |
| - | [[Category: Maturation]]
| + | |
| - | [[Category: Ntn hydrolase]]
| + | |
| - | [[Category: Post-translational processing]]
| + | |
| - | [[Category: Precursor]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
Q65KZ6_BACLD
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pica A, Chi MC, Chen YY, d'Ischia M, Lin LL, Merlino A. 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. Biochim Biophys Acta. 2015 Oct 30. pii: S1570-9639(15)00268-X. doi:, 10.1016/j.bbapap.2015.10.006. PMID:26536828 doi:http://dx.doi.org/10.1016/j.bbapap.2015.10.006
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