2ae4
From Proteopedia
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==Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism== | ==Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism== | ||
| - | <StructureSection load='2ae4' size='340' side='right' caption='[[2ae4]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2ae4' size='340' side='right'caption='[[2ae4]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ae4]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ae4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._GK16 Pseudomonas sp. GK16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AE4 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ae4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae4 OCA], [https://pdbe.org/2ae4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ae4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ae4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae4 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G7AC_PSEU7 G7AC_PSEU7] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA).<ref>PMID:2993240</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2ae4_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2ae4_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ae4 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ae4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through sequential primary and secondary autoproteolytic reactions with the release of a pro segment. We have determined crystal structures of four CA mutants. Two mutants are trapped after the primary cleavage, and the other two undergo secondary cleavage slowly. These structures provide a look at pro-segment conformation during activation in N-terminal nucleophile hydrolases. The highly strained helical pro segment of precursor is transformed into a relaxed loop in the intermediates, suggesting that the relaxation of structural constraints drives the primary cleavage reaction. The secondary autoproteolytic step has been proposed to be intermolecular. However, our analysis provides evidence that CA is processed in two sequential steps of intramolecular autoproteolysis involving two distinct residues in the active site, the first a serine and the second a glutamate. | ||
| - | + | ==See Also== | |
| - | + | *[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas sp. | + | [[Category: Pseudomonas sp. GK16]] |
| - | [[Category: Cho | + | [[Category: Cho KJ]] |
| - | [[Category: Kim | + | [[Category: Kim JK]] |
| - | [[Category: Kim | + | [[Category: Kim KH]] |
| - | [[Category: Kim | + | [[Category: Kim SH]] |
| - | [[Category: Park | + | [[Category: Park SS]] |
| - | [[Category: Ryu | + | [[Category: Ryu EK]] |
| - | [[Category: Shin | + | [[Category: Shin HJ]] |
| - | [[Category: Yang | + | [[Category: Yang IS]] |
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Current revision
Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism
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Categories: Large Structures | Pseudomonas sp. GK16 | Cho KJ | Kim JK | Kim KH | Kim SH | Park SS | Ryu EK | Shin HJ | Yang IS
