1ltx: Difference between revisions

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[[Image:1ltx.gif|left|200px]]
{{Seed}}
[[Image:1ltx.png|left|200px]]


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{{STRUCTURE_1ltx|  PDB=1ltx  |  SCENE=  }}  
{{STRUCTURE_1ltx|  PDB=1ltx  |  SCENE=  }}  


'''Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid'''
===Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid===




==Overview==
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Posttranslational geranylgeranylation of Rab GTPases is catalyzed by Rab geranylgeranyltransferase (RabGGTase), which consists of a catalytic alpha/beta heterodimer and an accessory Rab escort protein (REP). The crystal structure of isoprenoid-bound RabGGTase complexed to REP-1 has been solved to 2.7 A resolution. The complex interface buries a surprisingly small surface area of ca. 680 A and is unexpectedly formed by helices 8, 10, and 12 of the RabGGTase alpha subunit and helices D and E of REP-1. We demonstrate that the affinity of RabGGTase for REP-1 is allosterically regulated by phosphoisoprenoid via a long-range trans-domain signal transduction event. Comparing the structure of REP-1 with the closely related RabGDI, we conclude that the specificity of the REP:RabGGTase interaction is defined by differently positioned phenylalanine residues conserved in the REP and GDI subfamilies.
The line below this paragraph, {{ABSTRACT_PUBMED_12620235}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12620235 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12620235}}


==About this Structure==
==About this Structure==
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[[Category: Prenyltransferase]]
[[Category: Prenyltransferase]]
[[Category: Rab prenylation]]
[[Category: Rab prenylation]]
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