2irv: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2irv ConSurf].
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Revision as of 02:35, 8 February 2016

Crystal structure of GlpG, a rhomboid intramembrane serine proteaseCrystal structure of GlpG, a rhomboid intramembrane serine protease

Structural highlights

2irv is a 2 chain structure with sequence from Ecoli. The August 2011 RCSB PDB Molecule of the Month feature on Rhomboid Protease GlpG by David Goodsell is 10.2210/rcsb_pdb/mom_2011_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:glpG (ECOLI)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GLPG_ECOLI] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Wu Z, Yan N, Feng L, Oberstein A, Yan H, Baker RP, Gu L, Jeffrey PD, Urban S, Shi Y. Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nat Struct Mol Biol. 2006 Dec;13(12):1084-91. Epub 2006 Nov 10. PMID:17099694 doi:10.1038/nsmb1179
  2. ↑ Maegawa S, Ito K, Akiyama Y. Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Biochemistry. 2005 Oct 18;44(41):13543-52. PMID:16216077 doi:10.1021/bi051363k
  3. ↑ Ben-Shem A, Fass D, Bibi E. Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):462-6. Epub 2006 Dec 26. PMID:17190827

2irv, resolution 2.30Å

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