1uai: Difference between revisions
New page: left|200px<br /><applet load="1uai" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uai, resolution 1.20Å" /> '''Crystal Structure of... |
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[[Image:1uai.jpg|left|200px]]<br /><applet load="1uai" size=" | [[Image:1uai.jpg|left|200px]]<br /><applet load="1uai" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1uai, resolution 1.20Å" /> | caption="1uai, resolution 1.20Å" /> | ||
'''Crystal Structure of the Alginate Lyase from Corynebacterium sp.'''<br /> | '''Crystal Structure of the Alginate Lyase from Corynebacterium sp.'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of alginate (poly alpha-l-guluronate) lyase from | 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. | ||
==About this Structure== | ==About this Structure== | ||
1UAI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.]. Active as [http://en.wikipedia.org/wiki/Poly(alpha-L-guluronate)_lyase Poly(alpha-L-guluronate) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.11 4.2.2.11] Full crystallographic information is available from [http:// | 1UAI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.]. Active as [http://en.wikipedia.org/wiki/Poly(alpha-L-guluronate)_lyase Poly(alpha-L-guluronate) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.11 4.2.2.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: jellyroll beta-sandwich]] | [[Category: jellyroll beta-sandwich]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:20 2008'' | ||
Revision as of 16:22, 21 February 2008
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Crystal Structure of the Alginate Lyase from Corynebacterium sp.
OverviewOverview
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.
About this StructureAbout this Structure
1UAI is a Single protein structure of sequence from Corynebacterium sp.. Active as Poly(alpha-L-guluronate) lyase, with EC number 4.2.2.11 Full crystallographic information is available from OCA.
ReferenceReference
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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