1yzn
From Proteopedia
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|PDB= 1yzn |SIZE=350|CAPTION= <scene name='initialview01'>1yzn</scene>, resolution 2.06Å | |PDB= 1yzn |SIZE=350|CAPTION= <scene name='initialview01'>1yzn</scene>, resolution 2.06Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YPT1, YP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= YPT1, YP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yzn OCA], [http://www.ebi.ac.uk/pdbsum/1yzn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yzn RCSB]</span> | ||
}} | }} | ||
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[[Category: Pan, X.]] | [[Category: Pan, X.]] | ||
[[Category: Ritacco, C.]] | [[Category: Ritacco, C.]] | ||
| - | [[Category: GNP]] | ||
| - | [[Category: MG]] | ||
[[Category: protein transport]] | [[Category: protein transport]] | ||
[[Category: rab gtpase]] | [[Category: rab gtpase]] | ||
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[[Category: ypt1p gtpase]] | [[Category: ypt1p gtpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:26:55 2008'' |
Revision as of 22:26, 30 March 2008
| |||||||
| , resolution 2.06Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | YPT1, YP2 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GppNHp-Bound Ypt1p GTPase
Overview
Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations.
About this Structure
1YZN is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis of family-wide Rab GTPase recognition by rabenosyn-5., Eathiraj S, Pan X, Ritacco C, Lambright DG, Nature. 2005 Jul 21;436(7049):415-9. PMID:16034420
Page seeded by OCA on Mon Mar 31 01:26:55 2008
