2bme

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{{Seed}}
 
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[[Image:2bme.png|left|200px]]
 
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==high resolution structure of GppNHp-bound human Rab4a==
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The line below this paragraph, containing "STRUCTURE_2bme", creates the "Structure Box" on the page.
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<StructureSection load='2bme' size='340' side='right'caption='[[2bme]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bme]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BME FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.57&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_2bme| PDB=2bme | SCENE= }}
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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=2bme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bme OCA], [https://pdbe.org/2bme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bme RCSB], [https://www.ebi.ac.uk/pdbsum/2bme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bme ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RAB4A_HUMAN RAB4A_HUMAN] Protein transport. Probably involved in vesicular traffic (By similarity).
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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/bm/2bme_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=2bme ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Ras-related human GTPase Rab4a is involved in the regulation of endocytosis through the sorting and recycling of early endosomes. Towards further insight, we have determined the three-dimensional crystal structure of human Rab4a in its GppNHp-bound state to 1.6 Angstroms resolution and in its GDP-bound state to 1.8 Angstroms resolution, respectively. Despite the similarity of the overall structure with other Rab proteins, Rab4a displays significant differences. The structures are discussed with respect to the recently determined structure of human Rab5a and its complex with the Rab5-binding domain of the bivalent effector Rabaptin-5. The Rab4 specific residue His39 modulates the nucleotide binding pocket giving rise to a reduced rate for nucleotide hydrolysis and exchange. In comparison to Rab5, Rab4a has a different GDP-bound conformation within switch 1 region and displays shifts in position and orientation of the hydrophobic triad. The observed differences at the S2-L3-S3 region represent a new example of structural plasticity among Rab proteins and may provide a structural basis to understand the differential binding of similar effector proteins.
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===HIGH RESOLUTION STRUCTURE OF GPPNHP-BOUND HUMAN RAB4A===
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High resolution crystal structures of human Rab4a in its active and inactive conformations.,Huber SK, Scheidig AJ FEBS Lett. 2005 May 23;579(13):2821-9. Epub 2005 Apr 25. PMID:15907487<ref>PMID:15907487</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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The line below this paragraph, {{ABSTRACT_PUBMED_15907487}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2bme" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15907487 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15907487}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2BME is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BME OCA].
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==Reference==
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<ref group="xtra">PMID:15907487</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Small monomeric GTPase]]
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[[Category: Large Structures]]
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[[Category: Huber, S K.]]
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[[Category: Huber SK]]
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[[Category: Scheidig, A J.]]
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[[Category: Scheidig AJ]]
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[[Category: Endocytosis]]
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[[Category: Gtp-binding protein]]
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[[Category: Prenylation]]
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[[Category: Protein transport]]
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[[Category: Transport]]
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[[Category: Vesicular transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:45:50 2009''
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Current revision

high resolution structure of GppNHp-bound human Rab4a

PDB ID 2bme

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