Structural highlights
5k3c is a 2 chain structure with sequence from Rhopa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| NonStd Res: | |
| Related: | 5k3b, 5k3a, 5k3d, 5k3f, 5k3e |
| Gene: | RPA1163 (RHOPA) |
| Activity: | Haloacetate dehalogenase, with EC number 3.8.1.3 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[DEHA_RHOPA] Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has lower activity towards bromoacetate and chloroacetate.[1] [2]
Publication Abstract from PubMed
Freeze-trapping x-ray crystallography, nuclear magnetic resonance, and computational techniques reveal the distribution of states and their interconversion rates along the reaction pathway of a bacterial homodimeric enzyme, fluoroacetate dehalogenase (FAcD). The crystal structure of apo-FAcD exhibits asymmetry around the dimer interface and cap domain, priming one protomer for substrate binding. This asymmetry is dynamically averaged through conformational exchange on a millisecond time scale. During catalysis, the protomer conformational exchange rate becomes enhanced, the empty protomer exhibits increased local disorder, and water egresses. Computational studies identify allosteric pathways between protomers. Water release and enhanced dynamics associated with catalysis compensate for entropic losses from substrate binding while facilitating sampling of the transition state. The studies provide insights into how substrate-coupled allosteric modulation of structure and dynamics facilitates catalysis in a homodimeric enzyme.
The role of dimer asymmetry and protomer dynamics in enzyme catalysis.,Kim TH, Mehrabi P, Ren Z, Sljoka A, Ing C, Bezginov A, Ye L, Pomes R, Prosser RS, Pai EF Science. 2017 Jan 20;355(6322). pii: eaag2355. doi: 10.1126/science.aag2355. PMID:28104837[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chan PW, Yakunin AF, Edwards EA, Pai EF. Mapping the Reaction Coordinates of Enzymatic Defluorination. J Am Chem Soc. 2011 Apr 21. PMID:21510690 doi:10.1021/ja200277d
- ↑ Chan PW, Yakunin AF, Edwards EA, Pai EF. Mapping the Reaction Coordinates of Enzymatic Defluorination. J Am Chem Soc. 2011 Apr 21. PMID:21510690 doi:10.1021/ja200277d
- ↑ Kim TH, Mehrabi P, Ren Z, Sljoka A, Ing C, Bezginov A, Ye L, Pomes R, Prosser RS, Pai EF. The role of dimer asymmetry and protomer dynamics in enzyme catalysis. Science. 2017 Jan 20;355(6322). pii: eaag2355. doi: 10.1126/science.aag2355. PMID:28104837 doi:http://dx.doi.org/10.1126/science.aag2355
