Crystal Structure of the Alginate Lyase from Corynebacterium sp.Crystal Structure of the Alginate Lyase from Corynebacterium sp.

Structural highlights

1uai is a 1 chain structure with sequence from Corynebacterium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9RB42_9CORY

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. (ALY-1) was determined at 1.2A resolution using the MAD method and bromide ions. The structure of ALY-1 is abundant in beta-strands and has a deep cleft, similar to the jellyroll beta-sandwich found in 1,3-1,4-beta-glucanase. The structure suggests that alginate molecules may penetrate into the cleft to interact with the catalytic site of ALY-1. The reported crystal structure of another type of alginate lyase, A1-III, differs from that of ALY-1 in that it consists almost entirely of alpha-helical structure. Nevertheless, the putative catalytic residues in both enzymes are positioned in space in nearly identical arrangements. This finding suggests that both alginate lyases may have evolved through convergent evolution.

Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution.,Osawa T, Matsubara Y, Muramatsu T, Kimura M, Kakuta Y J Mol Biol. 2005 Feb 4;345(5):1111-8. Epub 2004 Dec 13. PMID:15644208[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Osawa T, Matsubara Y, Muramatsu T, Kimura M, Kakuta Y. Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution. J Mol Biol. 2005 Feb 4;345(5):1111-8. Epub 2004 Dec 13. PMID:15644208 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.081

1uai, resolution 1.20Å

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