PDBsum entry 4p02

Transferase

PDB id

4p02

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Contents

			Protein chains

					728 a.a.


					655 a.a.

			Ligands

					UNK-UNK-UNK-UNK- UNK-UNK-UNK-UNK- UNK


					BGC-BGC-BGC-BGC- BGC-BGC-BGC-BGC- BGC-BGC-BGC-BGC- BGC-BGC-BGC-BGC- BGC


					C2E ×2


					PLC ×4


					3PE

			Metals

					_MG

PDB id:

4p02

Links
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- MMDB
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- Proteopedia
- CATH
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- ProSAT

Name:

Transferase

Title:

Structure of bacterial cellulose synthase with cyclic-di-gmp bound.

Structure:

Cellulose synthase subunit a. Chain: a. Engineered: yes. Cellulose synthase subunit b. Chain: b. Engineered: yes. Unidentified peptide. Chain: d. Engineered: yes

Source:

Rhodobacter sphaeroides. Organism_taxid: 272943. Strain: 2.4.1. Gene: rsp_0333. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rsp_0332. Expression_system_taxid: 562

Resolution:

2.65Å

R-factor:

0.200

R-free:

0.230

Authors:

J.L.W.Morgan,J.T.Mcnamara,J.Zimmer

Key ref:

J.L.Morgan et al. (2014). Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP. Nat Struct Biol, 21, 489-496. PubMed id: 24704788 DOI: 10.1038/nsmb.2803

Date:

20-Feb-14

Release date:

09-Apr-14

PROCHECK

	Headers

	References

Protein chain

Q3J125 (Q3J125_RHOS4) - Cellulose synthase catalytic subunit [UDP-forming] from Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

Seq: Struc:

Seq: Struc:					788 a.a. 728 a.a.

Protein chain

Q3J126 (Q3J126_RHOS4) - Cyclic di-GMP-binding protein from Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

Seq: Struc:

Seq: Struc:					725 a.a. 655 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chain A: E.C.2.4.1.12 - cellulose synthase (UDP-forming).

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D- glucosyl](n+1) + UDP + H⁺

[(1->4)-beta-D-glucosyl](n)	+	UDP-alpha-D-glucose	=	[(1->4)-beta-D- glucosyl](n+1)	+	UDP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1038/nsmb.2803	Nat Struct Biol 21:489-496 (2014)
PubMed id: 24704788

Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.
J.L.Morgan, J.T.McNamara, J.Zimmer.

ABSTRACT

The bacterial signaling molecule cyclic di-GMP (c-di-GMP) stimulates the synthesis of bacterial cellulose, which is frequently found in biofilms. Bacterial cellulose is synthesized and translocated across the inner membrane by a complex of cellulose synthase BcsA and BcsB subunits. Here we present crystal structures of the c-di-GMP-activated BcsA-BcsB complex. The structures reveal that c-di-GMP releases an autoinhibited state of the enzyme by breaking a salt bridge that otherwise tethers a conserved gating loop that controls access to and substrate coordination at the active site. Disrupting the salt bridge by mutagenesis generates a constitutively active cellulose synthase. Additionally, the c-di-GMP-activated BcsA-BcsB complex contains a nascent cellulose polymer whose terminal glucose unit rests at a new location above BcsA's active site and is positioned for catalysis. Our mechanistic insights indicate how c-di-GMP allosterically modulates enzymatic functions.