1l7j
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aldose_1-epimerase Aldose 1-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.3 5.1.3.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldose_1-epimerase Aldose 1-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.3 5.1.3.3] </span> |
|GENE= GALM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | |GENE= GALM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1l7k|1L7K]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7j OCA], [http://www.ebi.ac.uk/pdbsum/1l7j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l7j RCSB]</span> | ||
}} | }} | ||
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[[Category: mutarotase]] | [[Category: mutarotase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:59:12 2008'' |
Revision as of 18:59, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GALM (Lactococcus lactis) | ||||||
| Activity: | Aldose 1-epimerase, with EC number 5.1.3.3 | ||||||
| Related: | 1L7K
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of galactose mutarotase from Lactococcus lactis (apo)
Overview
Galactose mutarotase plays a key role in normal galactose metabolism by catalyzing the interconversion of beta-D-galactose and alpha-D-galactose. Here we describe the three-dimensional architecture of galactose mutarotase from Lactococcus lactis determined to 1.9-A resolution. Each subunit of the dimeric enzyme displays a distinctive beta-sandwich motif. This tertiary structural element was first identified in beta-galactosidase and subsequently observed in copper amine oxidase, hyaluronate lyase, chondroitinase, and maltose phosphorylase. Two cis-peptides are found in each subunit, namely Pro(67) and Lys(136). The active site is positioned in a rather open cleft, and the electron density corresponding to the bound galactose unequivocally demonstrates that both anomers of the substrate are present in the crystalline enzyme. Those residues responsible for anchoring the sugar to the protein include Arg(71), His(96), His(170), Asp(243), and Glu(304). Both His(96) and His(170) are strictly conserved among mutarotase amino acid sequences determined thus far. The imidazole nitrogens of these residues are located within hydrogen bonding distance to the C-5 oxygen of galactose. Strikingly, the carboxylate group of Glu(304) is situated at approximately 2.7 A from the 1'-hydroxyl group of galactose, thereby suggesting its possible role as a general acid/base group.
About this Structure
1L7J is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
Reference
High resolution X-ray structure of galactose mutarotase from Lactococcus lactis., Thoden JB, Holden HM, J Biol Chem. 2002 Jun 7;277(23):20854-61. Epub 2002 Mar 20. PMID:11907040
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