2bme

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[[Image:2bme.gif|left|200px]]<br /><applet load="2bme" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bme.gif|left|200px]]
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caption="2bme, resolution 1.57&Aring;" />
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'''HIGH RESOLUTION STRUCTURE OF GPPNHP-BOUND HUMAN RAB4A'''<br />
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{{Structure
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|PDB= 2bme |SIZE=350|CAPTION= <scene name='initialview01'>2bme</scene>, resolution 1.57&Aring;
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2]
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|GENE=
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}}
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'''HIGH RESOLUTION STRUCTURE OF GPPNHP-BOUND HUMAN RAB4A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GNP:'>GNP</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BME OCA].
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2BME 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=2BME OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15907487 15907487]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15907487 15907487]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: vesicular transport]]
[[Category: vesicular transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:03:50 2008''

Revision as of 14:03, 20 March 2008

Image:2bme.gif


PDB ID 2bme

Drag the structure with the mouse to rotate
, resolution 1.57Å
Sites:
Ligands: , , and
Activity: Small monomeric GTPase, with EC number 3.6.5.2
Coordinates: save as pdb, mmCIF, xml



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. 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

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