1ksu: Difference between revisions
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[[Image:1ksu.gif|left|200px]] | [[Image:1ksu.gif|left|200px]] | ||
'''Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina''' | {{Structure | ||
|PDB= 1ksu |SIZE=350|CAPTION= <scene name='initialview01'>1ksu</scene>, resolution 2.Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=FUM:FUMARIC ACID'>FUM</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] | |||
|GENE= fcc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 Shewanella frigidimarina]) | |||
}} | |||
'''Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KSU is a [ | 1KSU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSU OCA]. | ||
==Reference== | ==Reference== | ||
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK, Biochemistry. 2002 Jul 9;41(27):8551-6. PMID:[http:// | Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK, Biochemistry. 2002 Jul 9;41(27):8551-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12093271 12093271] | ||
[[Category: Shewanella frigidimarina]] | [[Category: Shewanella frigidimarina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: h505y]] | [[Category: h505y]] | ||
''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 12:21:47 2008'' | ||
Revision as of 13:21, 20 March 2008
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| , resolution 2.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | fcc (Shewanella frigidimarina) | ||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina
OverviewOverview
The X-ray structure of the soluble fumarate reductase from Shewanella frigidimarina [Taylor, P., Pealing, S. L., Reid, G. A., Chapman, S. K., and Walkinshaw, M. D. (1999) Nat. Struct. Biol. 6, 1108-1112] clearly shows the presence of an internally bound sodium ion. This sodium ion is coordinated by one solvent water molecule (Wat912) and five backbone carbonyl oxygens from Thr506, Met507, Gly508, Glu534, and Thr536 in what is best described as octahedral geometry (despite the rather long distance from the sodium ion to the backbone oxygen of Met507 (3.1 A)). The water ligand (Wat912) is, in turn, hydrogen bonded to the imidazole ring of His505. This histidine residue is adjacent to His504, a key active-site residue thought to be responsible for the observed pK(a) of the enzyme. Thus, it is possible that His505 may be important in both maintaining the sodium site and in influencing the active site. Here we describe the crystallographic and kinetic characterization of the H505A and H505Y mutant forms of the Shewanella fumarate reductase. The crystal structures of both mutant forms of the enzyme have been solved to 1.8 and 2.0 A resolution, respectively. Both show the presence of the sodium ion in the equivalent position to that found in the wild-type enzyme. The structure of the H505A mutant shows the presence of two water molecules in place of the His505 side-chain which form part of a hydrogen-bonding network with Wat48, a ligand to the sodium ion. The structure of the H505Y mutant shows the hydroxyl group of the tyrosine side-chain hydrogen-bonding to a water molecule which is also a ligand to the sodium ion. Apart from these features, there are no significant structural alterations as a result of either substitution. Both the mutant enzymes are catalytically active but show markedly different pH profiles compared to the wild-type enzyme. At high pH (above 8.5), the wild type and mutant enzymes have very similar activities. However, at low pH (6.0), the H505A mutant enzyme is some 20-fold less active than wild-type. The combined crystallographic and kinetic results suggest that His505 is not essential for sodium binding but does affect catalytic activity perhaps by influencing the pK(a) of the adjacent His504.
About this StructureAbout this Structure
1KSU is a Single protein structure of sequence from Shewanella frigidimarina. Full crystallographic information is available from OCA.
ReferenceReference
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK, Biochemistry. 2002 Jul 9;41(27):8551-6. PMID:12093271
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