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4gqy

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==Crystal structure of CBSX2 in complex with AMP==
==Crystal structure of CBSX2 in complex with AMP==
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<StructureSection load='4gqy' size='340' side='right' caption='[[4gqy]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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<StructureSection load='4gqy' size='340' side='right'caption='[[4gqy]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gqy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GQY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gqy]] is a 4 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=4GQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GQY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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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]] 2.193&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g34120, CBSX2, CDCP1, F28A23.120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gqy OCA], [http://pdbe.org/4gqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gqy RCSB], [http://www.ebi.ac.uk/pdbsum/4gqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gqy ProSAT]</span></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=4gqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gqy OCA], [https://pdbe.org/4gqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gqy RCSB], [https://www.ebi.ac.uk/pdbsum/4gqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gqy ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CBSX2_ARATH CBSX2_ARATH]
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Cystathionine beta-synthase (CBS) domains are small intracellular modules that can act as binding domains for adenosine derivatives, and they may regulate the activity of associated enzymes or other functional domains. Among these, the single CBS domain-containing proteins, CBSXs, from Arabidopsis thaliana, have recently been identified as redox regulators of the thioredoxin system. Here, the crystal structure of CBSX2 in complex with adenosine monophosphate (AMP) is reported at 2.2A resolution. The structure of dimeric CBSX2 with bound-AMP is shown to be approximately flat, which is in stark contrast to the bent form of apo-CBSXs. This conformational change in quaternary structure is triggered by a local structural change of the unique alpha5 helix, and by moving each loop P into an open conformation to accommodate incoming ligands. Furthermore, subtle rearrangement of the dimer interface triggers movement of all subunits, and consequently, the bent structure of the CBSX2 dimer becomes a flat structure. This reshaping of the structure upon complex formation with adenosine-containing ligand provides evidence that ligand-induced conformational reorganization of antiparallel CBS domains is an important regulatory mechanism.
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Change in single cystathionine beta-synthase domain-containing protein from a bent to flat conformation upon adenosine monophosphate binding.,Jeong BC, Park SH, Yoo KS, Shin JS, Song HK J Struct Biol. 2013 Jul;183(1):40-6. doi: 10.1016/j.jsb.2013.04.013. Epub 2013, May 9. PMID:23664870<ref>PMID:23664870</ref>
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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 4gqy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Jeong, B C]]
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[[Category: Large Structures]]
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[[Category: Song, H K]]
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[[Category: Jeong BC]]
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[[Category: Cbs domain]]
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[[Category: Song HK]]
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[[Category: Chloroplast in plant]]
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[[Category: Protein binding]]
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[[Category: Thioredoxin]]
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Current revision

Crystal structure of CBSX2 in complex with AMP

PDB ID 4gqy

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