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3rdi

From Proteopedia

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Current revision (12:19, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3rdi' size='340' side='right'caption='[[3rdi]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
<StructureSection load='3rdi' size='340' side='right'caption='[[3rdi]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rdi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rdi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</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]] 2.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1il6|1il6]], [[1i5z|1i5z]], [[3qop|3qop]]</div></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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3rdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdi OCA], [https://pdbe.org/3rdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdi RCSB], [https://www.ebi.ac.uk/pdbsum/3rdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdi ProSAT]</span></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=3rdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdi OCA], [https://pdbe.org/3rdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdi RCSB], [https://www.ebi.ac.uk/pdbsum/3rdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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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[https://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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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 3rdi" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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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 JC]]
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[[Category: White, M A]]
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[[Category: White MA]]
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[[Category: Allostery]]
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[[Category: Dna binding cyclic amp]]
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[[Category: Dna binding protein]]
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[[Category: Transcription regulator]]
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Current revision

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

PDB ID 3rdi

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