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1ghd

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{{Seed}}
 
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[[Image:1ghd.png|left|200px]]
 
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==Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad phasing==
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The line below this paragraph, containing "STRUCTURE_1ghd", creates the "Structure Box" on the page.
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<StructureSection load='1ghd' size='340' side='right'caption='[[1ghd]], [[Resolution|resolution]] 2.40&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'>[[1ghd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._130 Pseudomonas sp. 130]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1ghd| PDB=1ghd | 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=1ghd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghd OCA], [https://pdbe.org/1ghd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghd RCSB], [https://www.ebi.ac.uk/pdbsum/1ghd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O86089_9PROT O86089_9PROT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gh/1ghd_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1ghd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130 (C130) was irreversibly inhibited in a time-dependent manner by two substrate analogs bearing side chains of variable length, namely 7beta-bromoacetyl aminocephalosporanic acid (BA-7-ACA) and 7beta-3-bromopropionyl aminocephalosporanic acid (BP-7-ACA). The inhibition of the enzyme with BA-7-ACA was attributable to reaction with a single amino acid residue within the beta-subunit proven by comparative matrix assisted laser desorption/ionization-time of flight mass spectrometry. Further mass spectrometric analysis demonstrated that the fourth tryptophan residue of the beta-subunit, Trp-B4, was alkylated by BA-7-ACA. By (1)H-(13)C HSQC spectroscopy of C130 labeled by BA-2-(13)C-7-ACA, it was shown that tryptophan residue(s) in the enzyme was alkylated, forming a carbon-carbon bond. Replacing Trp-B4 with other amino acid residues caused increases in K(m), decreases in k(cat), and instability of enzyme activity. None of the mutant enzymes except W-B4Y could be affinity-alkylated, but all were competitively inhibited by BA-7-ACA. Kinetic studies revealed that both BA-7-ACA and BP-7-ACA could specifically alkylate Trp-B4 of C130 as well as Tyr-B4 of the mutant W-B4Y. Because these alkylations were energy-requiring under physiological conditions, it is likely that the affinity labeling reactions were catalyzed by the C130 enzyme itself. The Trp-B4 residue is located in the middle of a characteristic alphabetabetaalpha sandwich structure. Therefore, a large conformational alteration during inhibitor binding and transition state formation is likely and suggests that a major conformational change is induced by substrate binding during the course of catalysis.
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===Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad phasing===
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Affinity alkylation of the Trp-B4 residue of the beta -subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130.,Huang X, Zeng R, Ding X, Mao X, Ding Y, Rao Z, Xie Y, Jiang W, Zhao G J Biol Chem. 2002 Mar 22;277(12):10256-64. Epub 2002 Jan 8. PMID:11782466<ref>PMID:11782466</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 1ghd" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11782466}}, adds the Publication Abstract to the page
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*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11782466 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11782466}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1GHD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_sp._130 Pseudomonas sp. 130]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHD OCA].
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==Reference==
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Affinity alkylation of the Trp-B4 residue of the beta -subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130., Huang X, Zeng R, Ding X, Mao X, Ding Y, Rao Z, Xie Y, Jiang W, Zhao G, J Biol Chem. 2002 Mar 22;277(12):10256-64. Epub 2002 Jan 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11782466 11782466]
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[[Category: Protein complex]]
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[[Category: Pseudomonas sp. 130]]
[[Category: Pseudomonas sp. 130]]
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[[Category: Bartlam, M.]]
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[[Category: Bartlam M]]
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[[Category: Ding, Y.]]
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[[Category: Ding Y]]
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[[Category: He, H.]]
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[[Category: He H]]
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[[Category: Jiang, F.]]
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[[Category: Jiang F]]
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[[Category: Jiang, W.]]
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[[Category: Jiang W]]
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[[Category: Liu, Y.]]
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[[Category: Liu Y]]
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[[Category: Mao, X.]]
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[[Category: Mao X]]
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[[Category: Rao, Z.]]
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[[Category: Rao Z]]
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[[Category: Tang, H.]]
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[[Category: Tang H]]
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[[Category: Ye, S.]]
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[[Category: Ye S]]
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[[Category: Zhang, S.]]
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[[Category: Zhang S]]
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[[Category: Zhao, G.]]
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[[Category: Zhao G]]
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[[Category: Cephalosporin acylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:17:16 2008''
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Current revision

Crystal structure of the glutaryl-7-aminocephalosporanic acid acylase by mad phasing

PDB ID 1ghd

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