1dce

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(New page: 200px<br /><applet load="1dce" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dce, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dce.gif|left|200px]]<br /><applet load="1dce" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dce, resolution 2.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN==
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BACKGROUND: Rab geranylgeranyltransferase (RabGGT) catalyzes the addition, of two geranylgeranyl groups to the C-terminal cysteine residues of Rab, proteins, which is crucial for membrane association and function of these, proteins in intracellular vesicular trafficking. Unlike protein, farnesyltransferase (FT) and type I geranylgeranyltransferase, which both, prenylate monomeric small G proteins or short peptides, RabGGT can, prenylate Rab only when Rab is in a complex with Rab escort protein (REP)., RESULTS: The crystal structure of rat RabGGT at 2.0 A resolution reveals, an assembly of four distinct structural modules. The beta subunit forms an, alpha-alpha barrel that contains most of the residues in the active site., The alpha subunit consists of a helical domain, an immunoglobulin, (Ig)-like domain, and a leucine-rich repeat (LRR) domain. The N-terminal, region of the alpha subunit binds to the active site in the beta subunit;, residue His2alpha directly coordinates a zinc ion. The prenyl-binding, pocket of RabGGT is deeper than that in FT. CONCLUSIONS: LRR and Ig, domains are often involved in protein-protein interactions; in RabGGT they, might participate in the recognition and binding of REP. The binding of, the N-terminal peptide of the alpha subunit to the active site suggests an, autoinhibition mechanism that might contribute to the inability of RabGGT, to recognize short peptides or Rab alone as its substrate. Replacement of, residues Trp102beta and Tyr154beta in FT by Ser48beta and Leu99beta, respectively, in RabGGT largely determine the different lipid-binding, specificities of the two enzymes.
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<StructureSection load='1dce' size='340' side='right'caption='[[1dce]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dce]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCE FirstGlance]. <br>
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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&#8491;</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=FME:N-FORMYLMETHIONINE'>FME</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'>[https://proteopedia.org/fgij/fg.htm?mol=1dce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dce OCA], [https://pdbe.org/1dce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dce RCSB], [https://www.ebi.ac.uk/pdbsum/1dce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dce ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGTA_RAT PGTA_RAT] Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dce_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1dce ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DCE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCE OCA].
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*[[Geranylgeranyl transferase 3D structures|Geranylgeranyl transferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution., Zhang H, Seabra MC, Deisenhofer J, Structure. 2000 Mar 15;8(3):241-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10745007 10745007]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Deisenhofer, H.]]
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[[Category: Deisenhofer H]]
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[[Category: Seabra, M.C.]]
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[[Category: Seabra MC]]
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[[Category: Zhang, H.]]
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[[Category: Zhang H]]
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[[Category: ZN]]
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[[Category: 2.0 a resolution]]
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[[Category: alpha subunit]]
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[[Category: beta subunit]]
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[[Category: crystal structure]]
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[[Category: n-formylmethionine]]
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[[Category: rab geranylgeranyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:10:03 2007''
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CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN

PDB ID 1dce

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