1uai

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{{STRUCTURE_1uai| PDB=1uai | SCENE= }}
{{STRUCTURE_1uai| PDB=1uai | SCENE= }}
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'''Crystal Structure of the Alginate Lyase from Corynebacterium sp.'''
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===Crystal Structure of the Alginate Lyase from Corynebacterium sp.===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15644208 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15644208}}
==About this Structure==
==About this Structure==
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[[Category: Kakuta, Y.]]
[[Category: Kakuta, Y.]]
[[Category: Jellyroll beta-sandwich]]
[[Category: Jellyroll beta-sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:58:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:35:55 2008''

Revision as of 01:35, 28 July 2008

Image:1uai.png

Template:STRUCTURE 1uai

Crystal Structure of the Alginate Lyase from Corynebacterium sp.

Template:ABSTRACT PUBMED 15644208

About this Structure

1UAI is a Single protein structure of sequence from Corynebacterium sp.. Full crystallographic information is available from OCA.

Reference

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

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