5XNR

Truncated AlyQ with CBM32 and alginate lyase domains

Summary for 5XNR

• Entry DOI: 10.2210/pdb5xnr/pdb
• Descriptor: AlyQ, CALCIUM ION, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: alginate lyase, cbm32, lyase
• Biological source: Persicobacter sp. CCB-QB2
• Total number of polymer chains: 1
• Total formula weight: 44196.85

Authors

Teh, A.H.,Sim, P.F. (deposition date: 2017-05-24, release date: 2018-06-13, Last modification date: 2023-11-22)

Primary citation

Sim, P.F.,Furusawa, G.,Teh, A.H.
Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2.
Sci Rep, 7:13656-13656, 2017

PubMed Abstract: AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains - a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32) domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). Although AlyQ can also act on polyguluronate (poly-G) and polymannuronate (poly-M), it is most active on alginate. Studies with truncated AlyQ showed that the CBM32 domain did not contribute to enhancing AlyQ's activity under the assayed conditions. Nevertheless, it could bind to cleaved but not intact alginate, indicating that the CBM32 domain recognises alginate termini. The crystal structure containing both CBM32 and catalytic domains show that they do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain, meanwhile, shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1. As Persicobacter sp. CCB-QB2 was unable to utilise alginate, AlyQ may function to help the bacterium degrade cell walls more efficiently.

PubMed: 29057942
DOI: 10.1038/s41598-017-13288-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)