3btp
From Proteopedia
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- | [[Image:3btp.png|left|200px]] | ||
- | + | ==Crystal structure of Agrobacterium tumefaciens VirE2 in complex with its chaperone VirE1: a novel fold and implications for DNA binding== | |
- | + | <StructureSection load='3btp' size='340' side='right'caption='[[3btp]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3btp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BTP FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=3btp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3btp OCA], [https://pdbe.org/3btp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3btp RCSB], [https://www.ebi.ac.uk/pdbsum/3btp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3btp ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/VIRE2_AGRFC VIRE2_AGRFC] Involved in DNA transformation; mediates the nuclear uptake of single-stranded DNA copies of the transferred DNA (T-DNA) element. Binds single-stranded but not double-stranded DNA regardless of nucleotide sequence composition.<ref>PMID:12124400</ref> <ref>PMID:17784072</ref> <ref>PMID:8637884</ref> | |
- | + | == 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/bt/3btp_consurf.spt"</scriptWhenChecked> | |
- | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
- | + | <text>to colour the structure by Evolutionary Conservation</text> | |
- | == | + | </jmolCheckbox> |
- | [[3btp]] is a 2 chain structure with sequence from [ | + | </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=3btp ConSurf]. |
+ | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
- | *[[DNA-binding protein VirE2 from Agrobacterium tumefaciens complexed with chaperone VirE1|DNA-binding protein VirE2 from Agrobacterium tumefaciens complexed with chaperone VirE1]] | ||
- | *[[HIV Protease Inhibitor Resistance Profile|HIV Protease Inhibitor Resistance Profile]] | ||
- | *[[Interactive 3D Complements in Proteopedia|Interactive 3D Complements in Proteopedia]] | ||
- | *[[Main Page Test|Main Page Test]] | ||
*[[VirE1-VirE2|VirE1-VirE2]] | *[[VirE1-VirE2|VirE1-VirE2]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: Agrobacterium | + | </StructureSection> |
- | [[Category: | + | [[Category: Agrobacterium fabrum str. C58]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Albeck S]] |
- | [[Category: | + | [[Category: Dym O]] |
- | [[Category: Unger | + | [[Category: Elbaum M]] |
- | + | [[Category: Unger T]] | |
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Current revision
Crystal structure of Agrobacterium tumefaciens VirE2 in complex with its chaperone VirE1: a novel fold and implications for DNA binding
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