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<StructureSection load='2iwm' size='340' side='right'caption='[[2iwm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2iwm' size='340' side='right'caption='[[2iwm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2iwm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14577 Atcc 14577]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IWM FirstGlance]. <br>
<table><tr><td colspan='2'>[[2iwm]] 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=2IWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pva|2pva]], [[3pva|3pva]]</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]] 2.5&#8491;</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=2iwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwm OCA], [https://pdbe.org/2iwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwm RCSB], [https://www.ebi.ac.uk/pdbsum/2iwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwm OCA], [http://pdbe.org/2iwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iwm RCSB], [http://www.ebi.ac.uk/pdbsum/2iwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2iwm 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=2iwm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2iwm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Penicillin acylase|Penicillin acylase]]
*[[Penicillin acylase|Penicillin acylase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 14577]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Penicillin amidase]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Chandra, P M]]
[[Category: Chandra PM]]
[[Category: Dodson, G]]
[[Category: Dodson G]]
[[Category: Suresh, C G]]
[[Category: Suresh CG]]
[[Category: Antibiotic resistance]]
[[Category: Autoproteolysis]]
[[Category: Hydrolase]]
[[Category: Penicillin]]
[[Category: Precursor]]
[[Category: Zymogen]]

Latest revision as of 17:27, 13 December 2023

precursor mutant Cys1Ser of Penicillin V Acylase from Bacillus sphaericusprecursor mutant Cys1Ser of Penicillin V Acylase from Bacillus sphaericus

Structural highlights

2iwm is a 4 chain structure with sequence from Lysinibacillus sphaericus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2iwm, resolution 2.50Å

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OCA
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