3mji

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Current revision (08:48, 7 February 2024) (edit) (undo)
 
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<StructureSection load='3mji' size='340' side='right'caption='[[3mji]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3mji' size='340' side='right'caption='[[3mji]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3mji]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14577 Atcc 14577]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3MJI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3mji]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3MJI FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pva|2pva]], [[3pva|3pva]], [[2quy|2quy]], [[2z71|2z71]], [[3mik|3mik]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mji OCA], [https://pdbe.org/3mji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mji RCSB], [https://www.ebi.ac.uk/pdbsum/3mji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mji ProSAT]</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=3mji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mji OCA], [https://pdbe.org/3mji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mji RCSB], [https://www.ebi.ac.uk/pdbsum/3mji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mji ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PAC_LYSSH PAC_LYSSH]] The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase.
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[https://www.uniprot.org/uniprot/PAC_LYSSH PAC_LYSSH] The enzyme catalyzes the conversion of penicillin to 6-aminopenicillanate The precursor, furthermore, acts as a self-processing peptidase that cleaves off the propeptide. All peptidase activity is lost on conversion to the mature peptidase.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3mji" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Penicillin acylase|Penicillin acylase]]
*[[Penicillin acylase|Penicillin acylase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14577]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Penicillin amidase]]
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[[Category: Lysinibacillus sphaericus]]
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[[Category: Dodson, G G]]
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[[Category: Dodson GG]]
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[[Category: Murshudov, G N]]
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[[Category: Murshudov GN]]
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[[Category: Pathak, M C]]
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[[Category: Pathak MC]]
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[[Category: Suresh, C G]]
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[[Category: Suresh CG]]
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[[Category: Amidase]]
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[[Category: Antibiotic resistance]]
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[[Category: Autoproteolysis]]
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[[Category: Catalysis]]
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[[Category: Hydrolase]]
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[[Category: Penicillin]]
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[[Category: Penicillin v acylase]]
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[[Category: Zymogen]]
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Current revision

Activation of catalytic cysteine without a base in a Mutant Penicillin Acylase Precursor

PDB ID 3mji

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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