2QF5 | pdb_00002qf5

High resolution structure of the major periplasmic domain from the cell shape-determining filament MreC (monoclinic form)


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyMreC-like 8090234 3002420 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AMreCe2qf5A1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrelF: MreCECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.40.10.340 Mainly Beta Beta Barrel Thrombin, subunit H Rod shape-determining protein MreC, domain 1CATH (4.3.0)
A2.40.10.350 Mainly Beta Beta Barrel Thrombin, subunit H Rod shape-determining protein MreC, domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF04085Rod shape-determining protein MreC, barrel core (MreC)Rod shape-determining protein MreC, barrel coreMreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped [1]. This entry represents the periplasmic core of these proteins which is ...MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped [1]. This entry represents the periplasmic core of these proteins which is composed of two six-stranded beta-barrels [1,2]. MreC self-associates into polar filaments [1]. The periplasmic part of MreC contains also a coiled-coil region which is involved in the formation of dimer essential for its function [3].
Domain