1ecx: Difference between revisions
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'''NIFS-LIKE PROTEIN''' | {{Structure | ||
|PDB= 1ecx |SIZE=350|CAPTION= <scene name='initialview01'>1ecx</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NIFS-LIKE PROTEIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ECX is a [ | 1ECX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECX OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly., Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R, J Mol Biol. 2000 Mar 24;297(2):451-64. PMID:[http:// | Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly., Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R, J Mol Biol. 2000 Mar 24;297(2):451-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10715213 10715213] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: c-s beta lyase]] | [[Category: c-s beta lyase]] | ||
[[Category: iron-sulfur-cluster synthesis]] | [[Category: iron-sulfur-cluster synthesis]] | ||
[[Category: plp-dependent | [[Category: plp-dependent enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:50 2008'' | ||
Revision as of 11:53, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
NIFS-LIKE PROTEIN
OverviewOverview
NifS-like proteins are ubiquitous, homodimeric, proteins which belong to the alpha-family of pyridoxal-5'-phoshate dependent enzymes. They are proposed to donate elementary sulphur, generated from cysteine, via a cysteinepersulphide intermediate during iron sulphur cluster biosynthesis, an important albeit not well understood process. Here, we report on the crystal structure of a NifS-like protein from the hyperthermophilic bacterium Thermotoga maritima (tmNifS) at 2.0 A resolution. The tmNifS is structured into two domains, the larger bearing the pyridoxal-5'-phosphate-binding active site, the smaller hosting the active site cysteine in the middle of a highly flexible loop, 12 amino acid residues in length. Once charged with sulphur the loop could possibly deliver S(0) directly to regions far remote from the protein. Based on the three-dimensional structures of the native as well as the substrate complexed form and on spectrophotometric results, a mechanism of sulphur activation is proposed. The His99, which stacks on top of the pyridoxal-5'-phosphate co-factor, is assigned a crucial role during the catalytic cycle by acting as an acid-base catalyst and is believed to have a pK(a) value depending on the co-factor redox state.
About this StructureAbout this Structure
1ECX is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly., Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R, J Mol Biol. 2000 Mar 24;297(2):451-64. PMID:10715213
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