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3mji
From Proteopedia
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| - | [[ | + | ==Activation of catalytic cysteine without a base in a Mutant Penicillin Acylase Precursor== |
| + | <StructureSection load='3mji' size='340' side='right' caption='[[3mji]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3mji]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MJI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MJI FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pva|2pva]], [[3pva|3pva]], [[2quy|2quy]], [[2z71|2z71]], [[3mik|3mik]]</td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mji OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mji RCSB], [http://www.ebi.ac.uk/pdbsum/3mji PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystallization of three catalytically inactive mutants of penicillin V acylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme. | ||
| - | + | Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants.,Chandra PM, Brannigan JA, Prabhune A, Pundle A, Turkenburg JP, Dodson GG, Suresh CG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):124-7. Epub 2004 Dec 24. PMID:16508111<ref>PMID:16508111</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Lysinibacillus sphaericus]] | [[Category: Lysinibacillus sphaericus]] | ||
[[Category: Penicillin amidase]] | [[Category: Penicillin amidase]] | ||
Revision as of 10:36, 28 May 2014
Activation of catalytic cysteine without a base in a Mutant Penicillin Acylase Precursor
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