2ffq: Difference between revisions

Line 1:

[[Image:2ffq.gif|left|200px]]<br />

[[Image:2ffq.gif|left|200px]]<br /><applet load="2ffq" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2ffq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2ffq, resolution 1.78Å" />

'''The crystal structure of human neuronal Rab6B in its active GTPgS-bound form'''<br />

==Overview==

The Rab small G-protein family plays important roles in eukaryotes as, regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to, GDP is coupled with association with and dissociation from membranes., Conformational changes related to their different nucleotide states, determine their effector specificity. The crystal structure of human, neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and, 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both, crystallized in space group P2(1)2(1)2(1), with similar unit-cell, parameters, allowing the comparison of both structures without packing, artifacts. Conformational changes between the inactive GDP and active, GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab, proteins, additional changes are observed in the Rab6 subfamily-specific, RabSF3 region that might contribute to the specificity of Rab6 for its, different effector proteins.

The Rab small G-protein family plays important roles in eukaryotes as regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to GDP is coupled with association with and dissociation from membranes. Conformational changes related to their different nucleotide states determine their effector specificity. The crystal structure of human neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both crystallized in space group P2(1)2(1)2(1), with similar unit-cell parameters, allowing the comparison of both structures without packing artifacts. Conformational changes between the inactive GDP and active GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab proteins, additional changes are observed in the Rab6 subfamily-specific RabSF3 region that might contribute to the specificity of Rab6 for its different effector proteins.

==About this Structure==

2FFQ 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 MG and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FFQ OCA].

2FFQ 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> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFQ OCA].

==Reference==

Line 21:

Line 20:

[[Category: protein-nucleotide complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:04:~~36 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:01 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2ffq.gif|left|200px]]<br />
+[[Image:2ffq.gif|left|200px]]<br /><applet load="2ffq" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2ffq" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2ffq, resolution 1.78&Aring;" />
 '''The crystal structure of human neuronal Rab6B in its active GTPgS-bound form'''<br />
 ==Overview==
-The Rab small G-protein family plays important roles in eukaryotes as, regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to, GDP is coupled with association with and dissociation from membranes., Conformational changes related to their different nucleotide states, determine their effector specificity. The crystal structure of human, neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and, 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both, crystallized in space group P2(1)2(1)2(1), with similar unit-cell, parameters, allowing the comparison of both structures without packing, artifacts. Conformational changes between the inactive GDP and active, GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab, proteins, additional changes are observed in the Rab6 subfamily-specific, RabSF3 region that might contribute to the specificity of Rab6 for its, different effector proteins.
+The Rab small G-protein family plays important roles in eukaryotes as regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to GDP is coupled with association with and dissociation from membranes. Conformational changes related to their different nucleotide states determine their effector specificity. The crystal structure of human neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both crystallized in space group P2(1)2(1)2(1), with similar unit-cell parameters, allowing the comparison of both structures without packing artifacts. Conformational changes between the inactive GDP and active GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab proteins, additional changes are observed in the Rab6 subfamily-specific RabSF3 region that might contribute to the specificity of Rab6 for its different effector proteins.
 ==About this Structure==
-FFQ 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 MG and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FFQ OCA].
+FFQ 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> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFQ OCA].
 ==Reference==
@@ Line 21: / Line 20: @@
 [[Category: protein-nucleotide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:04:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:01 2008''