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< | ==The crystal structure of L-Phe inhibited prephenate dehydratase from Chlorobium tepidum TLS== | ||
<StructureSection load='2qmx' size='340' side='right'caption='[[2qmx]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlte Chlte]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> | |||
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pheA, CT1666 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=194439 CHLTE])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Prephenate_dehydratase Prephenate dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.51 4.2.1.51] </span></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=2qmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmx OCA], [https://pdbe.org/2qmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmx RCSB], [https://www.ebi.ac.uk/pdbsum/2qmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmx ProSAT], [https://www.topsan.org/Proteins/MCSG/2qmx TOPSAN]</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/qm/2qmx_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=2qmx ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and solution while a PDT dimer can be regarded as a basic catalytic unit. The N-terminal PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In one PDT dimer two clefts are aligned to form an extended active site across the dimer interface. Similarly at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation. | |||
Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.,Tan K, Li H, Zhang R, Gu M, Clancy ST, Joachimiak A J Struct Biol. 2008 Apr;162(1):94-107. Epub 2007 Nov 29. PMID:18171624<ref>PMID:18171624</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2qmx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Chlte]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: | |||
[[Category: Prephenate dehydratase]] | [[Category: Prephenate dehydratase]] | ||
[[Category: Clancy, S | [[Category: Clancy, S]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Li, H | [[Category: Li, H]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Tan, K | [[Category: Tan, K]] | ||
[[Category: Apc86053]] | [[Category: Apc86053]] | ||
[[Category: Chlorobium tepidum tl]] | [[Category: Chlorobium tepidum tl]] | ||
| Line 39: | Line 47: | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: Pdt]] | [[Category: Pdt]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
Latest revision as of 11:25, 25 June 2021
The crystal structure of L-Phe inhibited prephenate dehydratase from Chlorobium tepidum TLSThe crystal structure of L-Phe inhibited prephenate dehydratase from Chlorobium tepidum TLS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and solution while a PDT dimer can be regarded as a basic catalytic unit. The N-terminal PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In one PDT dimer two clefts are aligned to form an extended active site across the dimer interface. Similarly at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation. Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.,Tan K, Li H, Zhang R, Gu M, Clancy ST, Joachimiak A J Struct Biol. 2008 Apr;162(1):94-107. Epub 2007 Nov 29. PMID:18171624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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