1ltx

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(New page: 200px<br /><applet load="1ltx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ltx, resolution 2.70&Aring;" /> '''Structure of Rab Esc...)
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[[Image:1ltx.gif|left|200px]]<br /><applet load="1ltx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ltx.gif|left|200px]]<br /><applet load="1ltx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ltx, resolution 2.70&Aring;" />
caption="1ltx, resolution 2.70&Aring;" />
'''Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid'''<br />
'''Structure of Rab Escort Protein-1 in complex with Rab geranylgeranyl transferase and isoprenoid'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1LTX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN, CL and FAR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTX OCA].
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1LTX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=FAR:'>FAR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTX OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Alexandrov, K.]]
[[Category: Alexandrov, K.]]
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[[Category: Goody, R.S.]]
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[[Category: Goody, R S.]]
[[Category: Niculae, A.]]
[[Category: Niculae, A.]]
[[Category: Pylypenko, O.]]
[[Category: Pylypenko, O.]]
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[[Category: Reents, R.]]
[[Category: Reents, R.]]
[[Category: Schlichting, I.]]
[[Category: Schlichting, I.]]
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[[Category: Thoma, N.H.]]
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[[Category: Thoma, N H.]]
[[Category: Waldmann, H.]]
[[Category: Waldmann, H.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: rab prenylation]]
[[Category: rab prenylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:52:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:25 2008''

Revision as of 11:48, 21 February 2008


1ltx, resolution 2.70Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1LTX is a Protein complex structure of sequences from Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase., Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K, Mol Cell. 2003 Feb;11(2):483-94. PMID:12620235

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