1w27: Difference between revisions

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{{Seed}}
[[Image:1w27.png|left|200px]]


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==Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum==
The line below this paragraph, containing "STRUCTURE_1w27", creates the "Structure Box" on the page.
<StructureSection load='1w27' size='340' side='right'caption='[[1w27]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#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=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>
{{STRUCTURE_1w27|  PDB=1w27  |  SCENE=  }}
<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/initialview03.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.


===PHENYLALANINE AMMONIA-LYASE (PAL) FROM PETROSELINUM CRISPUM===
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&reg;/PubMed&reg;, 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==
The line below this paragraph, {{ABSTRACT_PUBMED_15548745}}, adds the Publication Abstract to the page
*[[Aminomutase 3D structures|Aminomutase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15548745 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15548745}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1W27 is a 2 chains structure of sequences from [http://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].
 
==Reference==
<ref group="xtra">PMID:15548745</ref><references group="xtra"/>
[[Category: Petroselinum crispum]]
[[Category: Petroselinum crispum]]
[[Category: Phenylalanine ammonia-lyase]]
[[Category: Ritter H]]
[[Category: Ritter, H.]]
[[Category: Schulz GE]]
[[Category: Schulz, G E.]]
[[Category: Lyase]]
[[Category: Mio]]
[[Category: Phenylpropanoid metabolism]]
 
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Retrieved from "https://proteopedia.org/1w27"