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3q4i

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==Crystal structure of CDP-Chase in complex with Gd3+==
==Crystal structure of CDP-Chase in complex with Gd3+==
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<StructureSection load='3q4i' size='340' side='right' caption='[[3q4i]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3q4i' size='340' side='right'caption='[[3q4i]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q4i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q4I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q4i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q4I 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=GD3:GADOLINIUM+ION'>GD3</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]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q1p|3q1p]]</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=GD3:GADOLINIUM+ION'>GD3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC2032, BC_2032 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])</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=3q4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q4i OCA], [https://pdbe.org/3q4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q4i RCSB], [https://www.ebi.ac.uk/pdbsum/3q4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q4i ProSAT]</span></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=3q4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q4i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q4i RCSB], [http://www.ebi.ac.uk/pdbsum/3q4i PDBsum]</span></td></tr>
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</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/Q81EE8_BACCR Q81EE8_BACCR]
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A Nudix enzyme from Bacillus cereus (NCBI RefSeq accession no. NP_831800) catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. Here, we show that in addition, the enzyme has a 3'--&gt;5' RNA exonuclease activity. The structure of the free enzyme, determined to a 1.8-A resolution, shows that the enzyme is an asymmetric dimer. Each monomer consists of two domains, an N-terminal helical domain and a C-terminal Nudix domain. The N-terminal domain is placed relative to the C-terminal domain such as to result in an overall asymmetric arrangement with two distinct catalytic sites: one with an "enclosed" Nudix pyrophosphatase site and the other with a more open, less-defined cavity. Residues that may be important for determining the asymmetry are conserved among a group of uncharacterized Nudix enzymes from Gram-positive bacteria. Our data support a model where CDP-choline hydrolysis is catalyzed by the enclosed Nudix site and RNA exonuclease activity is catalyzed by the open site. CDP-Chase is the first identified member of a novel Nudix family in which structural asymmetry has a profound effect on the recognition of substrates.
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The Nudix Hydrolase CDP-Chase, a CDP-Choline Pyrophosphatase, Is an Asymmetric Dimer with Two Distinct Enzymatic Activities.,Duong-Ly KC, Gabelli SB, Xu W, Dunn CA, Schoeffield AJ, Bessman MJ, Amzel LM J Bacteriol. 2011 Jul;193(13):3175-85. Epub 2011 Apr 29. PMID:21531795<ref>PMID:21531795</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus cereus]]
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[[Category: Bacillus cereus ATCC 14579]]
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[[Category: Amzel, L M]]
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[[Category: Large Structures]]
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[[Category: Duong-Ly, K C]]
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[[Category: Amzel LM]]
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[[Category: Gabelli, S B]]
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[[Category: Duong-Ly KC]]
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[[Category: Asymmetric dimer]]
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[[Category: Gabelli SB]]
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[[Category: Cdp-choline pyrophosphatase]]
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[[Category: Hydrolase]]
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[[Category: Nudix hydrolase]]
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[[Category: Pyrophosphatase]]
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[[Category: Rna exonuclease]]
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Current revision

Crystal structure of CDP-Chase in complex with Gd3+

PDB ID 3q4i

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