3k3w
From Proteopedia
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==Thermostable Penicillin G acylase from Alcaligenes faecalis in orthorhombic form== | ==Thermostable Penicillin G acylase from Alcaligenes faecalis in orthorhombic form== | ||
| - | <StructureSection load='3k3w' size='340' side='right' caption='[[3k3w]], [[Resolution|resolution]] 3.31Å' scene=''> | + | <StructureSection load='3k3w' size='340' side='right'caption='[[3k3w]], [[Resolution|resolution]] 3.31Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3k3w]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3k3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K3W 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]] 3.31Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k3w OCA], [https://pdbe.org/3k3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k3w RCSB], [https://www.ebi.ac.uk/pdbsum/3k3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k3w 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/O34142_ALCFA O34142_ALCFA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/3k3w_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/3k3w_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | + | The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C222(1), with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 , and P4(1)2(1)2, with unit-cell parameters a = b = 85.6, c = 298.8 . Data were collected at 293 and the structure was determined using the molecular-replacement method. Like other penicillin acylases, AfPGA belongs to the N-terminal nucleophilic hydrolase superfamily, has undergone post-translational processing and has a serine as the N-terminal residue of the beta-chain. A disulfide bridge has been identified in the structure that was not found in the other two known penicillin G cylase structures. The presence of the disulfide bridge is perceived to be one factor that confers higher stability to this enzyme. | |
| - | + | Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis.,Varshney NK, Kumar RS, Ignatova Z, Prabhune A, Pundle A, Dodson E, Suresh CG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):273-7. Epub, 2012 Feb 15. PMID:22442220<ref>PMID:22442220</ref> | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Alcaligenes faecalis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Dodson | + | [[Category: Dodson E]] |
| - | [[Category: Ignatova | + | [[Category: Ignatova Z]] |
| - | [[Category: Kumar | + | [[Category: Kumar RS]] |
| - | [[Category: Suresh | + | [[Category: Suresh CG]] |
| - | [[Category: Varshney | + | [[Category: Varshney NK]] |
| - | + | ||
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Current revision
Thermostable Penicillin G acylase from Alcaligenes faecalis in orthorhombic form
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