3rou

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[[Image:3rou.jpg|left|200px]]
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==Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)==
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<StructureSection load='3rou' size='340' side='right' caption='[[3rou]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3rou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ROU 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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1il6|1il6]], [[1i5z|1i5z]], [[3qop|3qop]], [[3rdi|3rdi]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3357, cap, crp, csm, JW5702 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3rou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rou OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rou RCSB], [http://www.ebi.ac.uk/pdbsum/3rou PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CRP_ECOLI CRP_ECOLI]] This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP.<ref>PMID:2982847</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of a dimer of the Escherichia coli catabolite gene activator protein has been refined at 2.5 A resolution to a crystallographic R-factor of 20.7% starting with coordinates fitted to the map at 2.9 A resolution. The two subunits are in different conformations and each contains one bound molecule of the allosteric activator, cyclic AMP. The amino-terminal domain is linked to the smaller carboxy-terminal domain by a nine-residue hinge region that exists in different conformations in the two subunits, giving rise to approximately a 30 degree rotation between the positions of the small domains relative to the larger domains. The amino-terminal domain contains an antiparallel beta-roll structure in which the interstrand hydrogen bonding is well-determined. The beta-roll can be described as a long antiparallel beta-ribbon that folds into a right-handed supercoil and forms part of the cyclic AMP binding site. Each cyclic AMP molecule is in an anti conformation and has ionic and hydrogen bond interactions with both subunits.
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Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution.,Weber IT, Steitz TA J Mol Biol. 1987 Nov 20;198(2):311-26. PMID:2828639<ref>PMID:2828639</ref>
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The line below this paragraph, containing "STRUCTURE_3rou", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3rou| PDB=3rou | SCENE= }}
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===Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)===
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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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==See Also==
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*[[Catabolite gene activator protein|Catabolite gene activator protein]]
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The line below this paragraph, {{ABSTRACT_PUBMED_2828639}}, adds the Publication Abstract to the page
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== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 2828639 is the PubMed ID number.
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<references/>
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__TOC__
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{{ABSTRACT_PUBMED_2828639}}
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</StructureSection>
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==About this Structure==
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[[3rou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROU OCA].
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==Reference==
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<ref group="xtra">PMID:002828639</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Knapp, J.]]
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[[Category: Knapp, J]]
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[[Category: Lee, J C.]]
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[[Category: Lee, J C]]
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[[Category: White, M A.]]
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[[Category: White, M A]]
[[Category: Allostery]]
[[Category: Allostery]]
[[Category: Dna binding cyclic amp]]
[[Category: Dna binding cyclic amp]]
[[Category: Dna binding protein]]
[[Category: Dna binding protein]]
[[Category: Transcription regulator]]
[[Category: Transcription regulator]]

Revision as of 04:31, 25 December 2014

Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)

3rou, resolution 2.10Å

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