1d5c

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(New page: 200px<br /><applet load="1d5c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5c, resolution 2.30&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1d5c.gif|left|200px]]<br /><applet load="1d5c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1d5c, resolution 2.30&Aring;" />
caption="1d5c, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM RAB6 COMPLEXED WITH GDP'''<br />
'''CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM RAB6 COMPLEXED WITH GDP'''<br />
==Overview==
==Overview==
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Rab proteins are small Ras-like GTPases which play important roles in, regulating intracellular vesicle trafficking. The nucleotide-binding, domain of Rab6 from the malaria parasite Plasmodium falciparum was, crystallized with GDP bound to the active site. The MAD phasing technique, was used to determine the crystal structure to 2.3 A resolution., Comparisons of the structure of GDP-bound PfRab6 with the recently, determined structures of Rab3A in complex with either a GTP analog or with, GTP and Rabphillin present structural evidence supporting the traditional, model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues, homologous to those distinguishing human Rab6 isoforms, which differ in, binding to Rabkinesin-6 in human cells, are located next to the recognized, complementarity-determining region (CDR) and constitute a conceptual, broadening of that domain. Despite significant observable differences in, Golgi ultrastructure, the Rab6 core structure and switch mechanism appear, highly conserved when compared with murine Rab3a structures. A significant, difference between the PfRab6 and higher eukaryotic Rabs may be the lack, of CDR features that allow binding interactions with Rabkinesin-type, effectors.
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Rab proteins are small Ras-like GTPases which play important roles in regulating intracellular vesicle trafficking. The nucleotide-binding domain of Rab6 from the malaria parasite Plasmodium falciparum was crystallized with GDP bound to the active site. The MAD phasing technique was used to determine the crystal structure to 2.3 A resolution. Comparisons of the structure of GDP-bound PfRab6 with the recently determined structures of Rab3A in complex with either a GTP analog or with GTP and Rabphillin present structural evidence supporting the traditional model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues homologous to those distinguishing human Rab6 isoforms, which differ in binding to Rabkinesin-6 in human cells, are located next to the recognized complementarity-determining region (CDR) and constitute a conceptual broadening of that domain. Despite significant observable differences in Golgi ultrastructure, the Rab6 core structure and switch mechanism appear highly conserved when compared with murine Rab3a structures. A significant difference between the PfRab6 and higher eukaryotic Rabs may be the lack of CDR features that allow binding interactions with Rabkinesin-type effectors.
==About this Structure==
==About this Structure==
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1D5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5C OCA].
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1D5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5C OCA].
==Reference==
==Reference==
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[[Category: vesicular trafficking]]
[[Category: vesicular trafficking]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:32:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:07 2008''

Revision as of 10:13, 21 February 2008

Image:1d5c.gif

1d5c, resolution 2.30Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM RAB6 COMPLEXED WITH GDP

Overview

Rab proteins are small Ras-like GTPases which play important roles in regulating intracellular vesicle trafficking. The nucleotide-binding domain of Rab6 from the malaria parasite Plasmodium falciparum was crystallized with GDP bound to the active site. The MAD phasing technique was used to determine the crystal structure to 2.3 A resolution. Comparisons of the structure of GDP-bound PfRab6 with the recently determined structures of Rab3A in complex with either a GTP analog or with GTP and Rabphillin present structural evidence supporting the traditional model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues homologous to those distinguishing human Rab6 isoforms, which differ in binding to Rabkinesin-6 in human cells, are located next to the recognized complementarity-determining region (CDR) and constitute a conceptual broadening of that domain. Despite significant observable differences in Golgi ultrastructure, the Rab6 core structure and switch mechanism appear highly conserved when compared with murine Rab3a structures. A significant difference between the PfRab6 and higher eukaryotic Rabs may be the lack of CDR features that allow binding interactions with Rabkinesin-type effectors.

About this Structure

1D5C is a Single protein structure of sequence from Plasmodium falciparum with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the nucleotide-binding domain of Plasmodium falciparum rab6 in the GDP-bound form., Chattopadhyay D, Langsley G, Carson M, Recacha R, DeLucas L, Smith C, Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):937-44. PMID:10944329

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