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| | ==Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase== | | ==Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase== |
| - | <StructureSection load='1tb3' size='340' side='right' caption='[[1tb3]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='1tb3' size='340' side='right'caption='[[1tb3]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tb3]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TB3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TB3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tb3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TB3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gox|1gox]], [[1fcb|1fcb]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HAO3, HAOX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tb3 OCA], [https://pdbe.org/1tb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tb3 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1tb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tb3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tb3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HAOX2_RAT HAOX2_RAT]] Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids. | + | [https://www.uniprot.org/uniprot/HAOX2_RAT HAOX2_RAT] Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Glycolate oxidase|Glycolate oxidase]] | + | *[[Glycolate oxidase 3D structures|Glycolate oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Amar, D]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Barton, J D]] | + | [[Category: Amar D]] |
| - | [[Category: Chen, Z W]] | + | [[Category: Barton JD]] |
| - | [[Category: Cunane, L M]] | + | [[Category: Chen ZW]] |
| - | [[Category: Le, K H.D]] | + | [[Category: Cunane LM]] |
| - | [[Category: Lederer, F]] | + | [[Category: Le KHD]] |
| - | [[Category: Mathews, F S]] | + | [[Category: Lederer F]] |
| - | [[Category: Flavoprotein]]
| + | [[Category: Mathews FS]] |
| - | [[Category: Long chain alpha-hydroxy acid oxidase]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
HAOX2_RAT Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cunane LM, Barton JD, Chen ZW, Le KH, Amar D, Lederer F, Mathews FS. Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase. Biochemistry. 2005 Feb 8;44(5):1521-31. PMID:15683236 doi:10.1021/bi048616e
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