2e22
From Proteopedia
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| - | [[Image:2e22.jpg|left|200px]] | + | [[Image:2e22.jpg|left|200px]] |
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| - | '''Crystal structure of xanthan lyase in complex with mannose''' | + | {{Structure |
| + | |PDB= 2e22 |SIZE=350|CAPTION= <scene name='initialview01'>2e22</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Xanthan_lyase Xanthan lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.12 4.2.2.12] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of xanthan lyase in complex with mannose''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2E22 is a [ | + | 2E22 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E22 OCA]. |
==Reference== | ==Reference== | ||
| - | A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan., Maruyama Y, Mikami B, Hashimoto W, Murata K, Biochemistry. 2007 Jan 23;46(3):781-91. PMID:[http:// | + | A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan., Maruyama Y, Mikami B, Hashimoto W, Murata K, Biochemistry. 2007 Jan 23;46(3):781-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17223699 17223699] |
[[Category: Bacillus sp.]] | [[Category: Bacillus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: xanthan]] | [[Category: xanthan]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:34:15 2008'' |
Revision as of 14:34, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Xanthan lyase, with EC number 4.2.2.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of xanthan lyase in complex with mannose
Overview
Xanthan is a bacterial heteropolysaccharide composed of pentasaccharide repeating units, i.e., a cellobiose as a backbone and a trisaccharide consisting of two mannoses and one glucuronic acid as a side chain. Nonreducing terminal mannose residues of xanthan side chains are partially pyruvated. Bacillus sp. GL1 xanthan lyase, a member of polysaccharide lyase family 8, acts specifically on pyruvated side chains of xanthan and yields pyruvated mannose through a beta-elimination reaction by using a single Tyr255 residue as base and acid catalysts. Here we show structural factors for substrate recognition by xanthan lyase through X-ray crystallographic and mutational analyses. The enzyme accommodates mannose and pyruvated mannose at the -1 subsite, although both inhibitor and dissociation constants of the two monosaccharides indicated that the affinity of pyruvated mannose for xanthan lyase is much higher than that of mannose. The high affinity of pyruvated mannose is probably due to the formation of additional hydrogen bonds between the carboxyl group of pyruvated mannose and amino acid residues of Tyr315 and Arg612. Site-directed mutagenesis of the two residues demonstrated that Arg612 is a key residue in recognizing pyruvated mannose. Arg612 is located in the protruding loop covering the substrate, suggesting that the loop functions as a lid that is responsible for the proper accommodation of the substrate at the active site.
About this Structure
2E22 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan., Maruyama Y, Mikami B, Hashimoto W, Murata K, Biochemistry. 2007 Jan 23;46(3):781-91. PMID:17223699
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