1l7k

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|PDB= 1l7k |SIZE=350|CAPTION= <scene name='initialview01'>1l7k</scene>, resolution 1.95&Aring;
|PDB= 1l7k |SIZE=350|CAPTION= <scene name='initialview01'>1l7k</scene>, resolution 1.95&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|LIGAND= <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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|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]
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|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=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7k OCA], [http://www.ebi.ac.uk/pdbsum/1l7k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l7k RCSB]</span>
}}
}}
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[[Category: Holden, H M.]]
[[Category: Holden, H M.]]
[[Category: Thoden, J B.]]
[[Category: Thoden, J B.]]
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[[Category: GLA]]
 
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[[Category: NA]]
 
[[Category: epimerase]]
[[Category: epimerase]]
[[Category: galactose metabolism]]
[[Category: galactose metabolism]]
[[Category: mutarotase]]
[[Category: mutarotase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:59:11 2008''

Revision as of 18:59, 30 March 2008


PDB ID 1l7k

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: ,
Gene: GALM (Lactococcus lactis)
Activity: Aldose 1-epimerase, with EC number 5.1.3.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



x-ray structure of galactose mutarotase from Lactococcus lactis complexed with galactose


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

1L7K 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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