Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
The diffraction images which allowed the 2.1 Angstrom resolution structure determination of Escherichia coli ALAD co-crystallised with a non-covalently bound moiety of the product, porphobilinogen (PBG), are presented. The structure revealed that the pyrrole side chain amino group is datively bound to the active site zinc ion and that the PBG carboxylates interact with the enzyme via hydrogen bonds and salt-bridges with invariant residues. A number of hydrogen bond interactions that were previously observed in the structure of yeast ALAD with a cyclic intermediate resembling the product PBG appear to be weaker in the new structure suggesting that these interactions are only optimal in the transition state.
Protein crystallography, Structural Biology, Tetrapyrrole Biosynthesis
Norton, Edwin
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Erskine, Peter
69c13bdf-c4a8-41e7-bbee-74f52f4b3095
Wood, Steve
c21cde08-332e-4002-93e2-aad09a7f4ea9
Shoolingin-Jordan, Peter
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Cooper, Jonathan
812eb501-58ac-4357-8fd7-21f7b947f512
Norton, Edwin
00910b84-1247-475e-a413-65ff62127727
Erskine, Peter
69c13bdf-c4a8-41e7-bbee-74f52f4b3095
Wood, Steve
c21cde08-332e-4002-93e2-aad09a7f4ea9
Shoolingin-Jordan, Peter
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Cooper, Jonathan
812eb501-58ac-4357-8fd7-21f7b947f512
Norton, Edwin, Erskine, Peter, Wood, Steve, Shoolingin-Jordan, Peter and Cooper, Jonathan
(2016)
Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
Zenodo
doi:10.5281/zenodo.51560
[Dataset]
Abstract
The diffraction images which allowed the 2.1 Angstrom resolution structure determination of Escherichia coli ALAD co-crystallised with a non-covalently bound moiety of the product, porphobilinogen (PBG), are presented. The structure revealed that the pyrrole side chain amino group is datively bound to the active site zinc ion and that the PBG carboxylates interact with the enzyme via hydrogen bonds and salt-bridges with invariant residues. A number of hydrogen bond interactions that were previously observed in the structure of yeast ALAD with a cyclic intermediate resembling the product PBG appear to be weaker in the new structure suggesting that these interactions are only optimal in the transition state.
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Published date: 2016
Keywords:
Protein crystallography, Structural Biology, Tetrapyrrole Biosynthesis
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Local EPrints ID: 434481
URI: http://eprints.soton.ac.uk/id/eprint/434481
PURE UUID: fe46cdb5-9320-4001-abab-670b3e80e036
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Date deposited: 24 Sep 2019 16:31
Last modified: 26 Feb 2024 18:26
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Creator:
Edwin Norton
Creator:
Peter Erskine
Creator:
Steve Wood
Creator:
Jonathan Cooper
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