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| | ==Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain== | | ==Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain== |
| - | <StructureSection load='1tu3' size='340' side='right' caption='[[1tu3]], [[Resolution|resolution]] 2.31Å' scene=''> | + | <StructureSection load='1tu3' size='340' side='right'caption='[[1tu3]], [[Resolution|resolution]] 2.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tu3]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tu3]] is a 10 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=1TU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TU3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAB5A, RAB5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RABEP1, RABPT5, RABPT5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu3 OCA], [http://pdbe.org/1tu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu3 ProSAT]</span></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=1tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu3 OCA], [https://pdbe.org/1tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/RABE1_HUMAN RABE1_HUMAN]] Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A.<ref>PMID:8521472</ref> <ref>PMID:10698684</ref> <ref>PMID:11452015</ref> <ref>PMID:12773381</ref> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Li, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, J]] | + | [[Category: Li G]] |
| - | [[Category: Terzyan, S]] | + | [[Category: Liu J]] |
| - | [[Category: Zhai, P]] | + | [[Category: Terzyan S]] |
| - | [[Category: Zhang, X C]] | + | [[Category: Zhai P]] |
| - | [[Category: Zhu, G]] | + | [[Category: Zhang XC]] |
| - | [[Category: Effector-binding]]
| + | [[Category: Zhu G]] |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Rab5]]
| + | |
| - | [[Category: Rabaptin5]]
| + | |
| Structural highlights
Function
RAB5A_HUMAN Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and the C-terminal domain of effector Rabaptin5. The proteins form a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel coiled-coil Rabaptin5 homodimer in the middle. Two Rab5 molecules bind independently to the Rabaptin5 dimer using their switch and interswitch regions. The binding does not involve the Rab complementarity-determining regions. We also present the crystal structures of two distinct forms of GDP-Rab5 complexes, both of which are incompatible with Rabaptin5 binding. One has a dislocated and disordered switch I but a virtually intact switch II, whereas the other has its beta-sheet and both switch regions reorganized. Biochemical and functional analyses show that the crystallographically observed Rab5-Rabaptin5 complex also exists in solution, and disruption of this complex by mutation abrogates endosome fusion.
Structural basis of Rab5-Rabaptin5 interaction in endocytosis.,Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:15378032[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gauthier-Campbell C, Bredt DS, Murphy TH, El-Husseini Ael-D. Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs. Mol Biol Cell. 2004 May;15(5):2205-17. Epub 2004 Feb 20. PMID:14978216 doi:10.1091/mbc.E03-07-0493
- ↑ Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC. Structural basis of Rab5-Rabaptin5 interaction in endocytosis. Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:15378032 doi:10.1038/nsmb832
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