|
|
| Line 3: |
Line 3: |
| | <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 [http://en.wikipedia.org/wiki/Alcfa Alcfa]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K3W FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pac ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 ALCFA])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></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=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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k3w OCA], [http://pdbe.org/3k3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k3w RCSB], [http://www.ebi.ac.uk/pdbsum/3k3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k3w ProSAT]</span></td></tr> | + | |
| | </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]] |
| Line 35: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcfa]] | + | [[Category: Alcaligenes faecalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Penicillin amidase]]
| + | [[Category: Dodson E]] |
| - | [[Category: Dodson, E]] | + | [[Category: Ignatova Z]] |
| - | [[Category: Ignatova, Z]] | + | [[Category: Kumar RS]] |
| - | [[Category: Kumar, R S]] | + | [[Category: Suresh CG]] |
| - | [[Category: Suresh, C G]] | + | [[Category: Varshney NK]] |
| - | [[Category: Varshney, N K]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Penicillin g acylase]]
| + | |
| Structural highlights
Function
O34142_ALCFA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Varshney NK, Kumar RS, Ignatova Z, Prabhune A, Pundle A, Dodson E, Suresh CG. Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):273-7. Epub, 2012 Feb 15. PMID:22442220 doi:http://dx.doi.org/10.1107/S1744309111053930
|
