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==Crystal Structure of Threonine Synthase from Yeast==
The line below this paragraph, containing "STRUCTURE_1kl7", creates the "Structure Box" on the page.
<StructureSection load='1kl7' size='340' side='right'caption='[[1kl7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1kl7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KL7 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]] 2.7&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
{{STRUCTURE_1kl7|  PDB=1kl7  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kl7 OCA], [https://pdbe.org/1kl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kl7 ProSAT]</span></td></tr>
 
</table>
'''Crystal Structure of Threonine Synthase from Yeast'''
== Function ==
 
[https://www.uniprot.org/uniprot/THRC_YEAST THRC_YEAST] Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine (By similarity).
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Threonine synthase catalyzes the final step of threonine biosynthesis, the pyridoxal 5'-phosphate (PLP)-dependent conversion of O-phosphohomoserine into threonine and inorganic phosphate. Threonine is an essential nutrient for mammals, and its biosynthetic machinery is restricted to bacteria, plants, and fungi; therefore, threonine synthase represents an interesting pharmaceutical target. The crystal structure of threonine synthase from Saccharomyces cerevisiae has been solved at 2.7 A resolution using multiwavelength anomalous diffraction. The structure reveals a monomer as active unit, which is subdivided into three distinct domains: a small N-terminal domain, a PLP-binding domain that covalently anchors the cofactor and a so-called large domain, which contains the main of the protein body. All three domains show the typical open alpha/beta architecture. The cofactor is bound at the interface of all three domains, buried deeply within a wide canyon that penetrates the whole molecule. Based on structural alignments with related enzymes, an enzyme-substrate complex was modeled into the active site of yeast threonine synthase, which revealed essentials for substrate binding and catalysis. Furthermore, the comparison with related enzymes of the beta-family of PLP-dependent enzymes indicated structural determinants of the oligomeric state and thus rationalized for the first time how a PLP enzyme acts in monomeric form.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/1kl7_consurf.spt"</scriptWhenChecked>
1KL7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL7 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Structure and function of threonine synthase from yeast., Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T, J Biol Chem. 2002 Apr 5;277(14):12396-405. Epub 2001 Dec 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11756443 11756443]
</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=1kl7 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bourenkov GP]]
[[Category: Threonine synthase]]
[[Category: Clausen T]]
[[Category: Bourenkov, G P.]]
[[Category: Ehlert S]]
[[Category: Clausen, T.]]
[[Category: Garrido-Franco M]]
[[Category: Ehlert, S.]]
[[Category: Huber R]]
[[Category: Garrido-Franco, M.]]
[[Category: Laber B]]
[[Category: Huber, R.]]
[[Category: Marinkovic S]]
[[Category: Laber, B.]]
[[Category: Messerschmidt A]]
[[Category: Marinkovic, S.]]
[[Category: Messerschmidt, A.]]
[[Category: Beta-family]]
[[Category: Monomer]]
[[Category: Pyridoxal 5-phosphate]]
[[Category: Threonine synthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:52:27 2008''

Latest revision as of 11:01, 3 April 2024

Crystal Structure of Threonine Synthase from YeastCrystal Structure of Threonine Synthase from Yeast

Structural highlights

1kl7 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THRC_YEAST Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1kl7, resolution 2.70Å

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OCA
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