PDBsum entry 5c98

Unknown function

PDB id: 5c98

Contents

Protein chains

359 a.a.

Waters ×537

PDB id:

5c98

Name:

Unknown function

Title:

1.45a resolution structure of srpn18 from anopheles gambiae

Structure:

Agap007691-pb. Chain: a, b. Engineered: yes

Source:

Anopheles gambiae. African malaria mosquito. Organism_taxid: 7165. Gene: srpn18, agap_agap007691. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.45Å R-factor: 0.166 R-free: 0.185

Authors:

S.Lovell,K.P.Battaile,M.Gulley,X.Zhang,D.A.Meekins,F.P.Gao,K.Michel

Key ref:

D.A.Meekins et al. (2016). 1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae. Acta Crystallogr F Struct Biol Commun, 72, 853-862. PubMed id: 27917832

Date:

26-Jun-15 Release date: 14-Sep-16

Protein chains

A7UR55  (A7UR55_ANOGA) -  AGAP007691-PB from Anopheles gambiae

Seq: 391 a.a.

Struc: 359 a.a.

Acta Crystallogr F Struct Biol Commun 72:853-862 (2016)

PubMed id: 27917832

1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae.

D.A.Meekins, X.Zhang, K.P.Battaile, S.Lovell, K.Michel.

ABSTRACT

Serine protease inhibitors (serpins) in insects function within development, wound healing and immunity. The genome of the African malaria vector, Anopheles gambiae, encodes 23 distinct serpin proteins, several of which are implicated in disease-relevant physiological responses. A. gambiae serpin 18 (SRPN18) was previously categorized as non-inhibitory based on the sequence of its reactive-center loop (RCL), a region responsible for targeting and initiating protease inhibition. The crystal structure of A. gambiae SRPN18 was determined to a resolution of 1.45 Å, including nearly the entire RCL in one of the two molecules in the asymmetric unit. The structure reveals that the SRPN18 RCL is extremely short and constricted, a feature associated with noncanonical inhibitors or non-inhibitory serpin superfamily members. Furthermore, the SRPN18 RCL does not contain a suitable protease target site and contains a large number of prolines. The SRPN18 structure therefore reveals a unique RCL architecture among the highly conserved serpin fold.