1pmo
From Proteopedia
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|PDB= 1pmo |SIZE=350|CAPTION= <scene name='initialview01'>1pmo</scene>, resolution 2.3Å | |PDB= 1pmo |SIZE=350|CAPTION= <scene name='initialview01'>1pmo</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene> | + | |LIGAND= <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate_decarboxylase Glutamate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.15 4.1.1.15] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_decarboxylase Glutamate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.15 4.1.1.15] </span> |
|GENE= GADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= GADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pmm|1PMM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmo OCA], [http://www.ebi.ac.uk/pdbsum/1pmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pmo RCSB]</span> | ||
}} | }} | ||
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[[Category: Grutter, M G.]] | [[Category: Grutter, M G.]] | ||
[[Category: Gut, H.]] | [[Category: Gut, H.]] | ||
| - | [[Category: PLR]] | ||
| - | [[Category: TRS]] | ||
[[Category: neutral-ph form of gadb]] | [[Category: neutral-ph form of gadb]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:41 2008'' |
Revision as of 20:01, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | GADB (Escherichia coli) | ||||||
| Activity: | Glutamate decarboxylase, with EC number 4.1.1.15 | ||||||
| Related: | 1PMM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Escherichia coli GadB (neutral pH)
Overview
Glutamate decarboxylase is a vitamin B6-dependent enzyme, which catalyses the decarboxylation of glutamate to gamma-aminobutyrate. In Escherichia coli, expression of glutamate decarboxylase (GadB), a 330 kDa hexamer, is induced to maintain the physiological pH under acidic conditions, like those of the passage through the stomach en route to the intestine. GadB, together with the antiporter GadC, constitutes the gad acid resistance system, which confers the ability for bacterial survival for at least 2 h in a strongly acidic environment. GadB undergoes a pH-dependent conformational change and exhibits an activity optimum at low pH. We determined the crystal structures of GadB at acidic and neutral pH. They reveal the molecular details of the conformational change and the structural basis for the acidic pH optimum. We demonstrate that the enzyme is localized exclusively in the cytoplasm at neutral pH, but is recruited to the membrane when the pH falls. We show by structure-based site-directed mutagenesis that the triple helix bundle formed by the N-termini of the protein at acidic pH is the major determinant for this behaviour.
About this Structure
1PMO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase., Capitani G, De Biase D, Aurizi C, Gut H, Bossa F, Grutter MG, EMBO J. 2003 Aug 15;22(16):4027-37. PMID:12912902
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