2nrf: Difference between revisions

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[[Image:2nrf.gif|left|200px]]<br /><applet load="2nrf" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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

caption="2nrf, resolution 2.600Å" />

'''Crystal Structure of GlpG, a Rhomboid family intramembrane protease'''<br />

==Overview==

Intramembrane proteolysis regulates diverse biological processes. Cleavage, of substrate peptide bonds within the membrane bilayer is catalyzed by, integral membrane proteases. Here we report the crystal structure of the, transmembrane core domain of GlpG, a rhomboid-family intramembrane serine, protease from Escherichia coli. The protein contains six transmembrane, helices, with the catalytic Ser201 located at the N terminus of helix, alpha4 approximately 10 A below the membrane surface. Access to water, molecules is provided by a central cavity that opens to the extracellular, region and converges on Ser201. One of the two GlpG molecules in the, asymmetric unit has an open conformation at the active site, with the, transmembrane helix alpha5 bent away from the rest of the molecule., Structural analysis suggests that substrate entry to the active site is, probably gated by the movement of helix alpha5.

Intramembrane proteolysis regulates diverse biological processes. Cleavage of substrate peptide bonds within the membrane bilayer is catalyzed by integral membrane proteases. Here we report the crystal structure of the transmembrane core domain of GlpG, a rhomboid-family intramembrane serine protease from Escherichia coli. The protein contains six transmembrane helices, with the catalytic Ser201 located at the N terminus of helix alpha4 approximately 10 A below the membrane surface. Access to water molecules is provided by a central cavity that opens to the extracellular region and converges on Ser201. One of the two GlpG molecules in the asymmetric unit has an open conformation at the active site, with the transmembrane helix alpha5 bent away from the rest of the molecule. Structural analysis suggests that substrate entry to the active site is probably gated by the movement of helix alpha5.

==About this Structure==

2NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2NRF OCA].

2NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRF OCA].

==Reference==

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[[Category: integral membrane protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 12:51:~~51 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:04 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2nrf.gif|left|200px]]<br /><applet load="2nrf" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nrf.gif|left|200px]]<br /><applet load="2nrf" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2nrf, resolution 2.600&Aring;" />
 '''Crystal Structure of GlpG, a Rhomboid family intramembrane protease'''<br />
 ==Overview==
-Intramembrane proteolysis regulates diverse biological processes. Cleavage, of substrate peptide bonds within the membrane bilayer is catalyzed by, integral membrane proteases. Here we report the crystal structure of the, transmembrane core domain of GlpG, a rhomboid-family intramembrane serine, protease from Escherichia coli. The protein contains six transmembrane, helices, with the catalytic Ser201 located at the N terminus of helix, alpha4 approximately 10 A below the membrane surface. Access to water, molecules is provided by a central cavity that opens to the extracellular, region and converges on Ser201. One of the two GlpG molecules in the, asymmetric unit has an open conformation at the active site, with the, transmembrane helix alpha5 bent away from the rest of the molecule., Structural analysis suggests that substrate entry to the active site is, probably gated by the movement of helix alpha5.
+Intramembrane proteolysis regulates diverse biological processes. Cleavage of substrate peptide bonds within the membrane bilayer is catalyzed by integral membrane proteases. Here we report the crystal structure of the transmembrane core domain of GlpG, a rhomboid-family intramembrane serine protease from Escherichia coli. The protein contains six transmembrane helices, with the catalytic Ser201 located at the N terminus of helix alpha4 approximately 10 A below the membrane surface. Access to water molecules is provided by a central cavity that opens to the extracellular region and converges on Ser201. One of the two GlpG molecules in the asymmetric unit has an open conformation at the active site, with the transmembrane helix alpha5 bent away from the rest of the molecule. Structural analysis suggests that substrate entry to the active site is probably gated by the movement of helix alpha5.
 ==About this Structure==
-NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NRF OCA].
+NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRF OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: integral membrane protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:51:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:04 2008''