2nyf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2nyf" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2nyf.png|left|200px]]
+
==Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme==
 +
<StructureSection load='2nyf' size='340' side='right' caption='[[2nyf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2nyf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_punctiforme Nostoc punctiforme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYF OCA]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[1gkm|1gkm]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nyf RCSB], [http://www.ebi.ac.uk/pdbsum/2nyf PDBsum]</span></td></tr>
 +
<table>
 +
== 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/ny/2nyf_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
<!--
+
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>
-
The line below this paragraph, containing "STRUCTURE_2nyf", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_2nyf| PDB=2nyf | SCENE= }}
+
-
===Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_17240984}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 17240984 is the PubMed ID number.
+
</StructureSection>
-
-->
+
-
{{ABSTRACT_PUBMED_17240984}}
+
-
 
+
-
==About this Structure==
+
-
[[2nyf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_punctiforme Nostoc punctiforme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYF OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:017240984</ref><references group="xtra"/>
+
[[Category: Histidine ammonia-lyase]]
[[Category: Histidine ammonia-lyase]]
[[Category: Nostoc punctiforme]]
[[Category: Nostoc punctiforme]]

Revision as of 08:44, 7 May 2014

Crystal structure of phenylalanine ammonia-lyase from Nostoc punctiforme

2nyf, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nyf"
Views
Personal tools
Navigation
Toolbox