PDBsum entry 6fms

Hydrolase

PDB id: 6fms

Contents

Protein chains

157 a.a.

149 a.a.

Ligands

MLE-IIL-SER-ALO-5BV ×4

OLC ×22

Waters ×10

PDB id:

6fms

Name:

Hydrolase

Title:

Imisx-ep of se-lspa

Structure:

Lipoprotein signal peptidase. Chain: a, b, c, d. Synonym: prolipoprotein signal peptidase,signal peptidase ii,spase ii. Engineered: yes. Globomycin. Chain: e, f, g, h. Engineered: yes

Source:

Pseudomonas aeruginosa (strain atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1). Organism_taxid: 208964. Gene: lspa, ls, pa4559. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

3.00Å R-factor: 0.230 R-free: 0.271

Authors:

C.-Y.Huang,V.Olieric,N.Howe,R.Warshamanage,T.Weinert,E.Panepucci, L.Vogeley,S.Basu,K.Diederichs,M.Caffrey,M.Wang

Key ref:

C.Y.Huang et al. (2018). In situ serial crystallography for rapid de novo membrane protein structure determination. Commun Biol, 1, 124. PubMed id: 30272004

Date:

02-Feb-18 Release date: 29-Aug-18

Protein chains

Q9HVM5  (LSPA_PSEAE) -  Lipoprotein signal peptidase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 169 a.a.

Struc: 157 a.a.

Protein chains

Q9HVM5  (LSPA_PSEAE) -  Lipoprotein signal peptidase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 169 a.a.

Struc: 149 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.3.4.23.36 - signal peptidase Ii.
• Reaction: Cleavage of N-terminal leader sequences from membrane prolipoproteins. Hydrolyzes Xaa-Xbb-Xcc-|-Cys, in which Xaa is hydrophobic (preferably Leu), Xbb is often Ser or Ala, Xcc is often Gly or Ala, and the Cys is alkylated on sulfur with a diacylglyceryl group.

Commun Biol 1:124 (2018)

PubMed id: 30272004

In situ serial crystallography for rapid de novo membrane protein structure determination.

C.Y.Huang, V.Olieric, N.Howe, R.Warshamanage, T.Weinert, E.Panepucci, L.Vogeley, S.Basu, K.Diederichs, M.Caffrey, M.Wang.

ABSTRACT

De novo membrane protein structure determination is often limited by the availability of large crystals and the difficulties in obtaining accurate diffraction data for experimental phasing. Here we present a method that combines in situ serial crystallography with de novo phasing for fast, efficient membrane protein structure determination. The method enables systematic diffraction screening and rapid data collection from hundreds of microcrystals in in meso crystallization wells without the need for direct crystal harvesting. The requisite data quality for experimental phasing is achieved by accumulating diffraction signals from isomorphous crystals identified post-data collection. The method works in all experimental phasing scenarios and is particularly attractive with fragile, weakly diffracting microcrystals. The automated serial data collection approach can be readily adopted at most microfocus macromolecular crystallography beamlines.