Structural highlights
2zuv is a 2 chain structure with sequence from As 1.2186. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Related: | |
| Gene: | lnpA (AS 1.2186) |
| Activity: | 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase, with EC number 2.4.1.211 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[LNPA_BIFL2] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) from Bifidobacterium longum, a key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc- and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic beta-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates.
The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold.,Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kitaoka M, Tian J, Nishimoto M. Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum. Appl Environ Microbiol. 2005 Jun;71(6):3158-62. PMID:15933016 doi:71/6/3158
- ↑ Nishimoto M, Kitaoka M. Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum. Appl Environ Microbiol. 2007 Oct;73(20):6444-9. Epub 2007 Aug 24. PMID:17720833 doi:http://dx.doi.org/10.1128/AEM.01425-07
- ↑ Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold. J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470 doi:10.1074/jbc.M808525200
- ↑ Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold. J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470 doi:10.1074/jbc.M808525200
