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4n27

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==X-ray structure of Brucella abortus RicA==
==X-ray structure of Brucella abortus RicA==
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<StructureSection load='4n27' size='340' side='right' caption='[[4n27]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
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<StructureSection load='4n27' size='340' side='right'caption='[[4n27]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n27]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Brua2 Brua2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N27 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4n27]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N27 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=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.73&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAB1_1279, BruAb1_1263 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=359391 BRUA2])</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=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n27 OCA], [http://pdbe.org/4n27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n27 RCSB], [http://www.ebi.ac.uk/pdbsum/4n27 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n27 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=4n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n27 OCA], [https://pdbe.org/4n27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n27 RCSB], [https://www.ebi.ac.uk/pdbsum/4n27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n27 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/Q2YQG1_BRUA2 Q2YQG1_BRUA2]
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The Gram-negative intracellular pathogen Brucella abortus is the causative agent of brucellosis, which is among the most common zoonoses globally. The B. abortus RicA protein binds the host-expressed guanosine nucleotide-binding protein, Rab2, and modulates B. abortus infection biology. We have solved the first X-ray crystal structure of RicA to 2.7 A resolution and have quantified the affinity of RicA binding to human Rab2 in its GDP-bound and nucleotide-free forms. RicA adopts a classic gamma-carbonic anhydrase (gamma-CA) fold containing a left-handed beta-helix followed by a C-terminal alpha-helix. Two homotrimers of RicA occupy the crystallographic asymmetric unit. Though no zinc was included in the purification or crystallization buffers, zinc is contained within the RicA crystals, as demonstrated by X-ray fluorescence spectroscopy. Electron density for a Zn2+ ion coordinated by three histidine residues is evident in the putative active site of RicA. However, purified RicA preparations do not exhibit carbonic anhydrase activity, suggesting that Zn2+ may not be the physiologically relevant metal cofactor or that RicA is not a bona fide carbonic anhydrase enzyme. Isothermal titration calorimetry (ITC) measurements of purified RicA binding to purified human Rab2 and GDP-Rab2 revealed similar equilibrium affinities (Kd approximately 35 and 40 muM, respectively). This study thus defines RicA as a Zn2+-binding gamma-carbonic anhydrase-like protein that binds the human membrane fusion/trafficking protein Rab2 with low micromolar affinity in vitro. These results support a model in which gamma-CA family proteins may evolve unique cellular functions while retaining many of the structural hallmarks of archetypal gamma-CA enzymes.
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Molecular Structure of the Brucella abortus Metalloprotein RicA, a Rab2-Binding Virulence Effector.,Herrou J, Crosson S Biochemistry. 2013 Nov 22. PMID:24251537<ref>PMID:24251537</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 4n27" 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: Brua2]]
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[[Category: Brucella abortus 2308]]
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[[Category: Crosson, S]]
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[[Category: Large Structures]]
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[[Category: Herrou, J]]
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[[Category: Crosson S]]
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[[Category: Gamma carbonic anhydrase]]
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[[Category: Herrou J]]
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[[Category: Transferase]]
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[[Category: Zinc binding]]
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Current revision

X-ray structure of Brucella abortus RicA

PDB ID 4n27

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