2gmm
From Proteopedia
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|PDB= 2gmm |SIZE=350|CAPTION= <scene name='initialview01'>2gmm</scene>, resolution 2.15Å | |PDB= 2gmm |SIZE=350|CAPTION= <scene name='initialview01'>2gmm</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ukg|1UKG]], [[2gme|2GME]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmm OCA], [http://www.ebi.ac.uk/pdbsum/2gmm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gmm RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: legume lectin]] | [[Category: legume lectin]] | ||
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[[Category: sugar complex]] | [[Category: sugar complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:18:40 2008'' |
Revision as of 00:18, 31 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1UKG, 2GME
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-2)Man
Overview
The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.
About this Structure
2GMM is a Single protein structure of sequence from Pterocarpus angolensis. Full crystallographic information is available from OCA.
Reference
Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin., Garcia-Pino A, Buts L, Wyns L, Loris R, J Mol Biol. 2006 Aug 4;361(1):153-67. Epub 2006 Jun 21. PMID:16824540
Page seeded by OCA on Mon Mar 31 03:18:40 2008
