1ibj

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[[Image:1ibj.png|left|200px]]
 
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{{STRUCTURE_1ibj| PDB=1ibj | SCENE= }}
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==Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana==
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<StructureSection load='1ibj' size='340' side='right'caption='[[1ibj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ibj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#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=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ibj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibj OCA], [https://pdbe.org/1ibj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibj RCSB], [https://www.ebi.ac.uk/pdbsum/1ibj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/METC_ARATH METC_ARATH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ibj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ibj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The pyridoxal 5'-phosphate-dependent enzyme cystathionine beta-lyase (CBL) catalyzes the penultimate step in the de novo biosynthesis of Met in microbes and plants. Absence of CBL in higher organisms makes it an important target for the development of antibiotics and herbicides. The three-dimensional structure of cystathionine beta-lyase from Arabidopsis was determined by Patterson search techniques, using the structure of tobacco (Nicotiana tabacum) cystathionine gamma-synthase as starting point. At a resolution of 2.3 A, the model was refined to a final crystallographic R-factor of 24.9%. The overall structure is very similar to other pyridoxal 5'-phosphate-dependent enzymes of the gamma-family. Exchange of a few critical residues within the active site causes the different substrate preferences between Escherichia coli and Arabidopsis CBL. Loss of interactions at the alpha-carboxyl site is the reason for the poorer substrate binding of Arabidopsis CBL. In addition, the binding pocket of Arabidopsis CBL is larger than that of E. coli CBL, explaining the similar binding of L-cystathionine and L-djenkolate in Arabidopsis CBL in contrast to E. coli CBL, where the substrate binding site is optimized for the natural substrate cystathionine.
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===Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana===
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The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity.,Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A Plant Physiol. 2001 Jun;126(2):631-42. PMID:11402193<ref>PMID:11402193</ref>
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{{ABSTRACT_PUBMED_11402193}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ibj" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[1ibj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBJ OCA].
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*[[Cystathionine beta-lyase|Cystathionine beta-lyase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:011402193</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Cystathionine beta-lyase]]
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[[Category: Large Structures]]
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[[Category: Breitinger, U.]]
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[[Category: Breitinger U]]
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[[Category: Clausen, T.]]
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[[Category: Clausen T]]
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[[Category: Messerschmidt, A.]]
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[[Category: Messerschmidt A]]
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[[Category: Lyase]]
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[[Category: Methionine biosynthesis]]
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[[Category: Plp-dependent enzyme]]
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[[Category: Transsulfuration]]
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Current revision

Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana

PDB ID 1ibj

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