2irv

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(New page: 200px<br /><applet load="2irv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2irv, resolution 2.3&Aring;" /> '''Crystal structure of ...)
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[[Image:2irv.gif|left|200px]]<br /><applet load="2irv" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2irv.gif|left|200px]]<br /><applet load="2irv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2irv, resolution 2.3&Aring;" />
caption="2irv, resolution 2.3&Aring;" />
'''Crystal structure of GlpG, a rhomboid intramembrane serine protease'''<br />
'''Crystal structure of GlpG, a rhomboid intramembrane serine protease'''<br />
==Overview==
==Overview==
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Intramembrane proteases catalyze peptide bond cleavage of integral, membrane protein substrates. This activity is crucial for many biological, and pathological processes. Rhomboids are evolutionarily widespread, intramembrane serine proteases. Here, we present the 2.3-A-resolution, crystal structure of a rhomboid from Escherichia coli. The enzyme has six, transmembrane helices, five of which surround a short TM4, which starts, deep within the membrane at the catalytic serine residue. Thus, the, catalytic serine is in an externally exposed cavity, which provides a, hydrophilic environment for proteolysis. Our results reveal a mechanism to, enable water-dependent catalysis at the depth of the hydrophobic milieu of, the membrane and suggest how substrates gain access to the sequestered, rhomboid active site.
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Intramembrane proteases catalyze peptide bond cleavage of integral membrane protein substrates. This activity is crucial for many biological and pathological processes. Rhomboids are evolutionarily widespread intramembrane serine proteases. Here, we present the 2.3-A-resolution crystal structure of a rhomboid from Escherichia coli. The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed cavity, which provides a hydrophilic environment for proteolysis. Our results reveal a mechanism to enable water-dependent catalysis at the depth of the hydrophobic milieu of the membrane and suggest how substrates gain access to the sequestered rhomboid active site.
==About this Structure==
==About this Structure==
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2IRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, LDA, LMT and PGV as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IRV OCA].
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2IRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=LDA:'>LDA</scene>, <scene name='pdbligand=LMT:'>LMT</scene> and <scene name='pdbligand=PGV:'>PGV</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IRV OCA].
==Reference==
==Reference==
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[[Category: ser-his dyad]]
[[Category: ser-his dyad]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:25:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:13 2008''

Revision as of 15:55, 21 February 2008

Image:2irv.gif

2irv, resolution 2.3Å

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Crystal structure of GlpG, a rhomboid intramembrane serine protease

Overview

Intramembrane proteases catalyze peptide bond cleavage of integral membrane protein substrates. This activity is crucial for many biological and pathological processes. Rhomboids are evolutionarily widespread intramembrane serine proteases. Here, we present the 2.3-A-resolution crystal structure of a rhomboid from Escherichia coli. The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed cavity, which provides a hydrophilic environment for proteolysis. Our results reveal a mechanism to enable water-dependent catalysis at the depth of the hydrophobic milieu of the membrane and suggest how substrates gain access to the sequestered rhomboid active site.

About this Structure

2IRV is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for intramembrane proteolysis by rhomboid serine proteases., Ben-Shem A, Fass D, Bibi E, Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):462-6. Epub 2006 Dec 26. PMID:17190827

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