PDBsum entry 4xlx

Hydrolase

PDB id: 4xlx

Contents

Protein chains

288 a.a.

267 a.a.

Waters ×651

PDB id:

4xlx

Name:

Hydrolase

Title:

Crystal structure of bjks from bradyrhizobium japonicum

Structure:

Uncharacterized protein blr2150. Chain: a, b, c, d. Synonym: orf8. Engineered: yes

Source:

Bradyrhizobium diazoefficiens (strain jcm 10833 / iam 13628 / nbrc 14792 / usda 110). Organism_taxid: 224911. Strain: jcm 10833 / iam 13628 / nbrc 14792 / usda 110. Gene: blr2150. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.176 R-free: 0.220

Authors:

Y.Hu,Y.Zheng,T.P.Ko,W.Liu,R.T.Guo

Key ref:

W.Liu et al. (2014). Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum. Sci Rep, 4, 6214. PubMed id: 25269599 DOI: 10.1038/srep06214

Date:

20-May-13 Release date: 04-Feb-15

Protein chains

Q45222  (Y2150_BRADU) -  Uncharacterized protein blr2150 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

Seq: 300 a.a.

Struc: 288 a.a.

Protein chain

Q45222  (Y2150_BRADU) -  Uncharacterized protein blr2150 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

Seq: 300 a.a.

Struc: 267 a.a.

DOI no: 10.1038/srep06214

Sci Rep 4:6214 (2014)

PubMed id: 25269599

Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum.

W.Liu, X.Feng, Y.Zheng, C.H.Huang, C.Nakano, T.Hoshino, S.Bogue, T.P.Ko, C.C.Chen, Y.Cui, J.Li, I.Wang, S.T.Hsu, E.Oldfield, R.T.Guo.

ABSTRACT

We report the first X-ray crystal structure of ent-kaur-16-ene synthase from Bradyrhizobium japonicum, together with the results of a site-directed mutagenesis investigation into catalytic activity. The structure is very similar to that of the α domains of modern plant terpene cyclases, a result that is of interest since it has been proposed that many plant terpene cyclases may have arisen from bacterial diterpene cyclases. The ent-copalyl diphosphate substrate binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues. A bisphosphonate inhibitor binds to the same site. In the kaurene synthase from the moss Physcomitrella patens, 16-α-hydroxy-ent-kaurane as well as kaurene are produced since Leu and Tyr in the P. patens kaurene synthase active site are replaced by smaller residues enabling carbocation quenching by water. Overall, the results represent the first structure determination of a bacterial diterpene cyclase, providing insights into catalytic activity, as well as structural comparisons with diverse terpene synthases and cyclases which clearly separate the terpene cyclases from other terpene synthases having highly α-helical structures.