2gnt: Difference between revisions
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|PDB= 2gnt |SIZE=350|CAPTION= <scene name='initialview01'>2gnt</scene>, resolution 2.02Å | |PDB= 2gnt |SIZE=350|CAPTION= <scene name='initialview01'>2gnt</scene>, resolution 2.02Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ukg|1UKG]], [[2gme|2GME]], [[2gmm|2GMM]], [[2gmp|2GMP]], [[2gn3|2GN3]], [[2gnb|2GNB]], [[2gnm|2GNM]], [[2gnd|2GND]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gnt OCA], [http://www.ebi.ac.uk/pdbsum/2gnt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gnt RCSB]</span> | |||
}} | }} | ||
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[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: legume lectin]] | [[Category: legume lectin]] | ||
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[[Category: remetallization]] | [[Category: remetallization]] | ||
''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 03:19:09 2008'' | ||
Revision as of 03:19, 31 March 2008
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| , resolution 2.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1UKG, 2GME, 2GMM, 2GMP, 2GN3, 2GNB, 2GNM, 2GND
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)
OverviewOverview
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 StructureAbout this Structure
2GNT is a Single protein structure of sequence from Pterocarpus angolensis. Full crystallographic information is available from OCA.
ReferenceReference
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
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