PDBsum entry 6f3k

Peptide binding protein

PDB id: 6f3k

Contents

Protein chain

353 a.a.

Metals

_ZN ×2

PDB id:

6f3k

Name:

Peptide binding protein

Title:

Combined solid-state nmr, solution-state nmr and em data for structure determination of the tetrahedral aminopeptidase tet2 from p. Horikoshii

Structure:

Tetrahedral aminopeptidase. Chain: a. Synonym: tet aminopeptidase,leucyl aminopeptidase,phtet2. Engineered: yes

Source:

Pyrococcus horikoshii (strain atcc 700860 / dsm 12428 / jcm 9974 / nbrc 100139 / ot-3). Organism_taxid: 70601. Strain: atcc 700860 / dsm 12428 / jcm 9974 / nbrc 100139 / ot-3. Gene: frvx, ph1527. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

10 models

Authors:

D.F.Gauto,L.F.Estrozi,C.D.Schwieters,G.Effantin,P.Macek,R.Sounier, R.Kerfah,A.C.Sivertsen,J.P.Colletier,J.Boisbouvier,G.Schoehn, A.Favier,P.Schanda

Key ref:

D.F.Gauto et al. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nat Commun, 10, 2697. PubMed id: 31217444 DOI: 10.1038/s41467-019-10490-9

Date:

28-Nov-17 Release date: 14-Mar-18

Protein chain

O59196  (TET_PYRHO) -  Tetrahedral aminopeptidase from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: 353 a.a.

Struc: 353 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.11.- - ?????

DOI no: 10.1038/s41467-019-10490-9

Nat Commun 10:2697 (2019)

PubMed id: 31217444

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex.

D.F.Gauto, L.F.Estrozi, C.D.Schwieters, G.Effantin, P.Macek, R.Sounier, A.C.Sivertsen, E.Schmidt, R.Kerfah, G.Mas, J.P.Colletier, P.Güntert, A.Favier, G.Schoehn, P.Schanda, J.Boisbouvier.

ABSTRACT

Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available.