1m22

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[[Image:1m22.gif|left|200px]]
 
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==X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A==
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The line below this paragraph, containing "STRUCTURE_1m22", creates the "Structure Box" on the page.
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<StructureSection load='1m22' size='340' side='right'caption='[[1m22]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m22]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M22 FirstGlance]. <br>
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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]] 1.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
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{{STRUCTURE_1m22| PDB=1m22 | SCENE= }}
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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=1m22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m22 OCA], [https://pdbe.org/1m22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m22 RCSB], [https://www.ebi.ac.uk/pdbsum/1m22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m22 ProSAT]</span></td></tr>
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</table>
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'''X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q8RJN5_STEMA Q8RJN5_STEMA]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The peptide amidase from Stenotrophomonas maltophilia catalyses predominantly the hydrolysis of the C-terminal amide bond in peptide amides. Peptide bonds or amide functions in amino acid side-chains are not hydrolysed. This specificity makes peptide amidase (Pam) interesting for different biotechnological applications. Pam belongs to the amidase signature (AS) family. It is the first protein within this family whose tertiary structure has been solved. The structure of the native Pam has been determined with a resolution of 1.4A and in complex with the competitive inhibitor chymostatin at a resolution of 1.8A. Chymostatin, which forms acyl adducts with many serine proteases, binds non-covalently to this enzyme.Pam folds as a very compact single-domain protein. The AS sequence represents a core domain that is covered by alpha-helices. This AS domain contains the catalytic residues. It is topologically homologous to the phosphoinositol phosphatase domain.The structural data do not support the recently proposed Ser-Lys catalytic dyad mechanism for AS enzymes. Our results are in agreement with the role of Ser226 as the primary nucleophile but differ concerning the roles of Ser202 and Lys123: Ser202, with direct contact both to the substrate molecule and to Ser226, presumably serves as an acid/bases catalyst. Lys123, with direct contact to Ser202 but no contact to Ser226 or the substrate molecule, most likely acts as an acid catalyst.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m22_consurf.spt"</scriptWhenChecked>
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1M22 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M22 OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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An alternative mechanism for amidase signature enzymes., Labahn J, Neumann S, Buldt G, Kula MR, Granzin J, J Mol Biol. 2002 Oct 4;322(5):1053-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12367528 12367528]
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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=1m22 ConSurf].
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[[Category: Single protein]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Stenotrophomonas maltophilia]]
[[Category: Stenotrophomonas maltophilia]]
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[[Category: Buldt, G.]]
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[[Category: Buldt G]]
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[[Category: Granzin, J.]]
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[[Category: Granzin J]]
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[[Category: Kula, M R.]]
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[[Category: Kula M-R]]
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[[Category: Labahn, J.]]
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[[Category: Labahn J]]
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[[Category: Neumann, S.]]
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[[Category: Neumann S]]
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[[Category: Covered double layers of alpha helices on top and bottom]]
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[[Category: Eleven-stranded beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:32:27 2008''
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Current revision

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A

PDB ID 1m22

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