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[[Image:1n6p.jpg|left|200px]]


{{Structure
==Crystal Structure of Human Rab5a A30E mutant complex with GppNHp==
|PDB= 1n6p |SIZE=350|CAPTION= <scene name='initialview01'>1n6p</scene>, resolution 1.54&Aring;
<StructureSection load='1n6p' size='340' side='right'caption='[[1n6p]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
<table><tr><td colspan='2'>[[1n6p]] is a 1 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=1N6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N6P FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1n6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6p OCA], [https://pdbe.org/1n6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6p RCSB], [https://www.ebi.ac.uk/pdbsum/1n6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RAB5A_HUMAN RAB5A_HUMAN] Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension.<ref>PMID:14978216</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n6/1n6p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1n6p ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of Human Rab5a A30E mutant complex with GppNHp'''
==See Also==
 
*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
 
== References ==
==Overview==
<references/>
GTPase domain crystal structures of Rab5a wild type and five variants with mutations in the phosphate-binding loop are reported here at resolutions up to 1.5 A. Of particular interest, the A30P mutant was crystallized in complexes with GDP, GDP+AlF(3), and authentic GTP, respectively. The other variant crystals were obtained in complexes with a non-hydrolyzable GTP analog, GppNHp. All structures were solved in the same crystal form, providing an unusual opportunity to compare structures of small GTPases with different catalytic rates. The A30P mutant exhibits dramatically reduced GTPase activity and forms a GTP-bound complex stable enough for crystallographic analysis. Importantly, the A30P structure with bound GDP plus AlF(3) has been solved in the absence of a GTPase-activating protein, and it may resemble that of a transition state intermediate. Conformational changes are observed between the GTP-bound form and the transition state intermediate, mainly in the switch II region containing the catalytic Gln(79) residue and independent of A30P mutation-induced local alterations in the P-loop. The structures suggest an important catalytic role for a P-loop backbone amide group, which is eliminated in the A30P mutant, and support the notion that the transition state of GTPase-mediated GTP hydrolysis is of considerable dissociative character.
__TOC__
 
</StructureSection>
==About this Structure==
1N6P is a [[Single protein]] structure of sequence 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=1N6P OCA].
 
==Reference==
High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop., Zhu G, Liu J, Terzyan S, Zhai P, Li G, Zhang XC, J Biol Chem. 2003 Jan 24;278(4):2452-60. Epub 2002 Nov 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12433916 12433916]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Li, G.]]
[[Category: Li G]]
[[Category: Liu, J.]]
[[Category: Liu J]]
[[Category: Terzyan, S.]]
[[Category: Terzyan S]]
[[Category: Zhai, P.]]
[[Category: Zhai P]]
[[Category: Zhang, X C.]]
[[Category: Zhang XC]]
[[Category: Zhu, G.]]
[[Category: Zhu G]]
[[Category: GNP]]
[[Category: MG]]
[[Category: gtpase]]
[[Category: rab]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:54 2008''

Latest revision as of 07:53, 14 February 2024

Crystal Structure of Human Rab5a A30E mutant complex with GppNHp

1n6p, resolution 1.54Å

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