PDBsum entry 6nxh

Transcription/inhibitor

PDB id: 6nxh

Contents

Protein chain

253 a.a.

Ligands

L8A

SO4 ×2

Metals

_BR

Waters ×103

PDB id:

6nxh

Name:

Transcription/inhibitor

Title:

Crystal structure of rar-related orphan receptor c (nhis- rorgt(244- 487)-l6-src1(678-692)) in complex with a phenyl (3-phenylpyrrolidin- 3-yl)sulfone inhibitor

Structure:

Nuclear receptor ror-gamma, nuclear receptor coactivator 1 chimera. Chain: a. Fragment: ligand-binding domain (unp residues 265-508) fused to src peptide (unp residues 683-696). Synonym: nuclear receptor rzr-gamma, nuclear receptor subfamily 1 group f member 3, rar-related orphan receptor c, retinoid-related orphan receptor-gamma,ncoa-1, class e basic helix-loop-helix protein 74, bhlhe74, protein hin-2, rip160, renal carcinoma antigen ny-ren-

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rorc, nr1f3, rorg, rzrg, ncoa1, bhlhe74, src1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.195 R-free: 0.239

Authors:

J.Sack

Key ref:

J.Greenfield et al. (2019). Structure and tailspike glycosidase machinery of ORF212 from E. coli O157:H7 phage CBA120 (TSP3). Sci Rep, 9, 7349. PubMed id: 31089181 DOI: 10.1038/s41598-019-43748-9

Date:

08-Feb-19 Release date: 13-Mar-19

Protein chain

P51449  (RORG_HUMAN) -  Nuclear receptor ROR-gamma from Homo sapiens

Seq: 518 a.a.

Struc: 253 a.a.*

Protein chain

Q15788  (NCOA1_HUMAN) -  Nuclear receptor coactivator 1 from Homo sapiens

Seq: 1441 a.a.

Struc: 253 a.a.*

* PDB and UniProt seqs differ at 239 residue positions (black crosses)

DOI no: 10.1038/s41598-019-43748-9

Sci Rep 9:7349 (2019)

PubMed id: 31089181

Structure and tailspike glycosidase machinery of ORF212 from E. coli O157:H7 phage CBA120 (TSP3).

J.Greenfield, X.Shang, H.Luo, Y.Zhou, R.D.Heselpoth, D.C.Nelson, O.Herzberg.

ABSTRACT

Bacteriophage tailspike proteins mediate virion absorption through reversible primary receptor binding, followed by lipopolysaccharide or exopolysaccharide degradation. The Escherichia coli O157:H7 bacteriophage CBA120 genome encodes four distinct tailspike proteins, annotated as ORFs 210 through 213. Previously, we reported the crystal structure of ORF210 (TSP1). Here we describe the crystal structure of ORF212 (TSP3) determined at 1.85 Å resolution. As observed with other tailspike proteins, TSP3 assembles into a trimer. Each subunit of TSP3 has an N-terminal head domain that is structurally similar to that of TSP1, consistent with their high amino acid sequence identity. In contrast, despite sharing a β-helix fold, the overall structure of the C-terminal catalytic domain of TSP3 is quite different when compared to TSP1. The TSP3 structure suggests that the glycosidase active site resides in a cleft at the interface between two adjacent subunits where three acidic residues, Glu362 and Asp383 on one subunit, and Asp426 on a second subunit, are located in close proximity. Comparing the glycosidase activity of wild-type TSP3 to various point mutants revealed that catalysis requires the carboxyl groups of Glu362 and Asp426, and not of Asp383, confirming the enzyme employs two carboxyl groups to degrade lippopolysaccharide using an acid/base mechanism.