1tb3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1tb3.gif|left|200px]]
{{Seed}}
[[Image:1tb3.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tb3|  PDB=1tb3  |  SCENE=  }}  
{{STRUCTURE_1tb3|  PDB=1tb3  |  SCENE=  }}  


'''Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase'''
===Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase===




==Overview==
<!--  
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.
The line below this paragraph, {{ABSTRACT_PUBMED_15683236}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15683236 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15683236}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15683236 15683236]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15683236 15683236]
Refined structure of spinach glycolate oxidase at 2 A resolution., Lindqvist Y, J Mol Biol. 1989 Sep 5;209(1):151-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2681790 2681790]
Molecular structure of flavocytochrome b2 at 2.4 A resolution., Xia ZX, Mathews FS, J Mol Biol. 1990 Apr 20;212(4):837-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2329585 2329585]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 32: Line 40:
[[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 Sat May  3 09:45:13 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:04:10 2008''
Retrieved from "https://proteopedia.org/1tb3"