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1w27
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="1w27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w27, resolution 1.70Å" /> '''PHENYLALANINE AMMON...) |
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| - | [[Image:1w27.gif|left|200px]]<br /> | ||
| - | <applet load="1w27" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1w27, resolution 1.70Å" /> | ||
| - | '''PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM'''<br /> | ||
| - | == | + | ==Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum== |
| - | Because of its key role in secondary phenylpropanoid metabolism, Phe | + | <StructureSection load='1w27' size='340' side='right'caption='[[1w27]], [[Resolution|resolution]] 1.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1w27]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Petroselinum_crispum Petroselinum crispum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W27 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w27 OCA], [https://pdbe.org/1w27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w27 RCSB], [https://www.ebi.ac.uk/pdbsum/1w27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w27 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PAL1_PETCR PAL1_PETCR] This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w2/1w27_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1w27 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Because of its key role in secondary phenylpropanoid metabolism, Phe ammonia-lyase is one of the most extensively studied plant enzymes. To provide a basis for detailed structure-function studies, the enzyme from parsley (Petroselinum crispum) was crystallized, and the structure was elucidated at 1.7-A resolution. It contains the unusual electrophilic 4-methylidene-imidazole-5-one group, which is derived from a tripeptide segment in two autocatalytic dehydration reactions. The enzyme resembles His ammonia-lyase from the general His degradation pathway but contains 207 additional residues, mainly in an N-terminal extension rigidifying a domain interface and in an inserted alpha-helical domain restricting the access to the active center. Presumably, Phe ammonia-lyase developed from His ammonia-lyase when fungi and plants diverged from the other kingdoms. A pathway of the catalyzed reaction is proposed in agreement with established biochemical data. The inactivation of the enzyme by a nucleophile is described in detail. | ||
| - | + | Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.,Ritter H, Schulz GE Plant Cell. 2004 Dec;16(12):3426-36. Epub 2004 Nov 17. PMID:15548745<ref>PMID:15548745</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1w27" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Aminomutase 3D structures|Aminomutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Petroselinum crispum]] | ||
| + | [[Category: Ritter H]] | ||
| + | [[Category: Schulz GE]] | ||
Current revision
Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum
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