![[Main Page]](/wiki/logos/proteopedia_135x200px_v1.01_15Years.png)
2bme
(Difference between revisions)
Categories: Homo sapiens | Single protein | Small monomeric GTPase | Huber, S K. | Scheidig, A J. | BME | GNP | MG | TRS | Endocytosis | Gtp-binding protein | Prenylation | Protein transport | Transport | Vesicular transport
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The Ras-related human GTPase Rab4a is involved in the regulation of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Small monomeric GTPase]] | [[Category: Small monomeric GTPase]] | ||
| - | [[Category: Huber, S | + | [[Category: Huber, S K.]] |
| - | [[Category: Scheidig, A | + | [[Category: Scheidig, A J.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: GNP]] | [[Category: GNP]] | ||
| Line 27: | Line 27: | ||
[[Category: vesicular transport]] | [[Category: vesicular transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:18 2008'' |
Revision as of 14:39, 21 February 2008
|
HIGH RESOLUTION STRUCTURE OF GPPNHP-BOUND HUMAN RAB4A
Overview
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.
About this Structure
2BME is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Small monomeric GTPase, with EC number 3.6.5.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:39:18 2008