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6SLL

Diaminobutyrate acetyltransferase EctA from Paenibacillus lautus in complex with its substrate L-2,4-diaminobutyric acid (DAB) and coenzyme A

Summary for 6SLL
Entry DOI10.2210/pdb6sll/pdb
DescriptorL-2,4-diaminobutyric acid acetyltransferase, COENZYME A, 2,4-DIAMINOBUTYRIC ACID, ... (5 entities in total)
Functional Keywordsl-2, 4-diaminobutyrate acetyltransferase, acetyl coenzyme a, acetylation, stress response, chemical chaperone, transferase
Biological sourceGeobacillus sp. (strain Y412MC10)
Total number of polymer chains2
Total formula weight43450.44
Authors
Richter, A.A.,Kobus, S.,Czech, L.,Hoeppner, A.,Bremer, E.,Smits, S.H.J. (deposition date: 2019-08-20, release date: 2020-01-29, Last modification date: 2024-01-24)
Primary citationRichter, A.A.,Kobus, S.,Czech, L.,Hoeppner, A.,Zarzycki, J.,Erb, T.J.,Lauterbach, L.,Dickschat, J.S.,Bremer, E.,Smits, S.H.J.
The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.
J.Biol.Chem., 295:2822-2838, 2020
Cited by
PubMed: 31969391
DOI: 10.1074/jbc.RA119.011277
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.2 Å)
Structure validation

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