1tb3: Difference between revisions
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|PDB= 1tb3 |SIZE=350|CAPTION= <scene name='initialview01'>1tb3</scene>, resolution 2.3Å | |PDB= 1tb3 |SIZE=350|CAPTION= <scene name='initialview01'>1tb3</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] </span> | ||
|GENE= HAO3, HAOX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= HAO3, HAOX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1gox|1GOX]], [[1fcb|1FCB]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tb3 OCA], [http://www.ebi.ac.uk/pdbsum/1tb3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tb3 RCSB]</span> | |||
}} | }} | ||
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[[Category: Lederer, F.]] | [[Category: Lederer, F.]] | ||
[[Category: Mathews, F S.]] | [[Category: Mathews, F S.]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
[[Category: long chain alpha-hydroxy acid oxidase]] | [[Category: long chain alpha-hydroxy acid oxidase]] | ||
[[Category: oxidase]] | [[Category: oxidase]] | ||
''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 23:53:44 2008'' | ||
Revision as of 23:53, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | HAO3, HAOX3 (Rattus norvegicus) | ||||||
| Activity: | (S)-2-hydroxy-acid oxidase, with EC number 1.1.3.15 | ||||||
| Related: | 1GOX, 1FCB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase
OverviewOverview
Long chain hydroxy acid oxidase (LCHAO) is a member of an FMN-dependent enzyme family that oxidizes L-2-hydroxy acids to ketoacids. LCHAO is a peroxisomal enzyme, and the identity of its physiological substrate is unclear. Mandelate is the most efficient substrate known and is commonly used in the test tube. LCHAO differs from most family members in that one of the otherwise invariant active site residues is a phenylalanine (Phe23) instead of a tyrosine. We now report the crystal structure of LCHAO. It shows the same beta8alpha8 TIM barrel structure as other structurally characterized family members, e.g., spinach glycolate oxidase (GOX) and the electron transferases yeast flavocytochrome b2 (FCB2) and Pseudomonas putida mandelate dehydrogenase (MDH). Loop 4, which is mobile in other family members, is visible in part. An acetate ion is present in the active site. The flavin interacts with the protein in the same way as in the electron transferases, and not as in GOX, an unexpected observation. An interpretation is proposed to explain this difference between GOX on one hand and FCB2 and LCHAO on the other hand, which had been proposed to arise from the differences between family members in their reactivity with oxygen. A comparison of models of the substrate bound to various published structures suggests that the very different reactivity with mandelate of LCHAO, GOX, FCB2, and MDH cannot be rationalized by a hydride transfer mechanism.
About this StructureAbout this Structure
1TB3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase., Cunane LM, Barton JD, Chen ZW, Le KH, Amar D, Lederer F, Mathews FS, Biochemistry. 2005 Feb 8;44(5):1521-31. PMID:15683236
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