1ay3: Difference between revisions
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|PDB= 1ay3 |SIZE=350|CAPTION= <scene name='initialview01'>1ay3</scene> | |PDB= 1ay3 |SIZE=350|CAPTION= <scene name='initialview01'>1ay3</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MFD:(2S,3S,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-10-PHENYLDECA-4,6-DIENOIC ACID'>MFD</scene> | |LIGAND= <scene name='pdbligand=ACB:3-METHYL-ASPARTIC+ACID'>ACB</scene>, <scene name='pdbligand=MDH:N-METHYLDEHYDROBUTYRINE'>MDH</scene>, <scene name='pdbligand=MFD:(2S,3S,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-10-PHENYLDECA-4,6-DIENOIC+ACID'>MFD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ay3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ay3 OCA], [http://www.ebi.ac.uk/pdbsum/1ay3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ay3 RCSB]</span> | |||
}} | }} | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Annila, A J.]] | [[Category: Annila, A J.]] | ||
[[Category: hepatotoxin]] | [[Category: hepatotoxin]] | ||
[[Category: inhibitor of ser/thr-specific protein phosphatase]] | [[Category: inhibitor of ser/thr-specific protein phosphatase]] | ||
''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 18:49:49 2008'' | ||
Revision as of 15:49, 30 March 2008
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| 1ay3 | |||||||||||||
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| Ligands: | ACB, MDH, MFD | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
NODULARIN FROM NODULARIA SPUMIGENA
Overview
The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level.
About this Structure
1AY3 is a Protein complex structure of sequences from Nodularia spumigena. Full crystallographic information is available from OCA.
Reference
Solution structure of nodularin. An inhibitor of serine/threonine-specific protein phosphatases., Annila A, Lehtimaki J, Mattila K, Eriksson JE, Sivonen K, Rantala TT, Drakenberg T, J Biol Chem. 1996 Jul 12;271(28):16695-702. PMID:8663277
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