2nyn

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[[Image:2nyn.gif|left|200px]]
 
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{{Structure
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==Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis==
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|PDB= 2nyn |SIZE=350|CAPTION= <scene name='initialview01'>2nyn</scene>, resolution 1.90&Aring;
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<StructureSection load='2nyn' size='340' side='right'caption='[[2nyn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-5-HYDROXY-4-METHYL-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene>
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<table><tr><td colspan='2'>[[2nyn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichormus_variabilis Trichormus variabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NYN FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3] </span>
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></td></tr>
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|DOMAIN=
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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=2nyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyn OCA], [https://pdbe.org/2nyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nyn RCSB], [https://www.ebi.ac.uk/pdbsum/2nyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nyn ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2nyf|2nyf]], [[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[1gkm|1gkm]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyn OCA], [http://www.ebi.ac.uk/pdbsum/2nyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nyn RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PAL_TRIV2 PAL_TRIV2] Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.<ref>PMID:17240984</ref> <ref>PMID:18556022</ref>
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== Evolutionary Conservation ==
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'''Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/2nyn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2nyn 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 ==
Phenylalanine ammonia lyase (PAL) catalyzes the deamination of phenylalanine to cinnamate and ammonia. While PALs are common in terrestrial plants where they catalyze the first committed step in the formation of phenylpropanoids, only a few prokaryotic PALs have been identified to date. Here we describe for the first time PALs from cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc punctiforme ATCC 29133, identified by screening the genome sequences of these organisms for members of the aromatic amino acid ammonia lyase family. Both PAL genes associate with secondary metabolite biosynthetic gene clusters as observed for other eubacterial PAL genes. In comparison to eukaryotic homologues, the cyanobacterial PALs are 20% smaller in size but share similar substrate selectivity and kinetic activity toward L-phenylalanine over L-tyrosine. Structure elucidation by protein X-ray crystallography confirmed that the two cyanobacterial PALs are similar in tertiary and quatenary structure to plant and yeast PALs as well as the mechanistically related histidine ammonia lyases.
Phenylalanine ammonia lyase (PAL) catalyzes the deamination of phenylalanine to cinnamate and ammonia. While PALs are common in terrestrial plants where they catalyze the first committed step in the formation of phenylpropanoids, only a few prokaryotic PALs have been identified to date. Here we describe for the first time PALs from cyanobacteria, in particular, Anabaena variabilis ATCC 29413 and Nostoc punctiforme ATCC 29133, identified by screening the genome sequences of these organisms for members of the aromatic amino acid ammonia lyase family. Both PAL genes associate with secondary metabolite biosynthetic gene clusters as observed for other eubacterial PAL genes. In comparison to eukaryotic homologues, the cyanobacterial PALs are 20% smaller in size but share similar substrate selectivity and kinetic activity toward L-phenylalanine over L-tyrosine. Structure elucidation by protein X-ray crystallography confirmed that the two cyanobacterial PALs are similar in tertiary and quatenary structure to plant and yeast PALs as well as the mechanistically related histidine ammonia lyases.
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==About this Structure==
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Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization.,Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS Biochemistry. 2007 Jan 30;46(4):1004-12. PMID:17240984<ref>PMID:17240984</ref>
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2NYN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_variabilis Anabaena variabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization., Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS, Biochemistry. 2007 Jan 30;46(4):1004-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17240984 17240984]
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</div>
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[[Category: Anabaena variabilis]]
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<div class="pdbe-citations 2nyn" style="background-color:#fffaf0;"></div>
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[[Category: Histidine ammonia-lyase]]
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[[Category: Single protein]]
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[[Category: Bowman, M E.]]
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[[Category: Louie, G V.]]
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[[Category: Moffitt, M C.]]
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[[Category: Moore, B S.]]
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[[Category: Noel, J P.]]
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[[Category: Pence, J.]]
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[[Category: methylidene imidazolone prosthetic group]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:10:18 2008''
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==See Also==
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*[[Aminomutase 3D structures|Aminomutase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Trichormus variabilis]]
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[[Category: Bowman ME]]
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[[Category: Louie GV]]
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[[Category: Moffitt MC]]
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[[Category: Moore BS]]
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[[Category: Noel JP]]
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[[Category: Pence J]]

Current revision

Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis

PDB ID 2nyn

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