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| - | [[Image:1zq6.gif|left|200px]]<br /><applet load="1zq6" size="450" color="white" frame="true" align="right" spinBox="true" | + | #REDIRECT [[3kzn]] This PDB entry is obsolete and replaced by 3kzn |
| - | caption="1zq6, resolution 1.80Å" />
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| - | '''Crystal Structure of N-acetyl-L-ornithine transcarbamylase complexed with N-acetyl-L-ornithine'''<br />
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| - | ==Overview==
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| - | N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the, transcarbamoylase superfamily that is essential for arginine biosynthesis, in several eubacteria. We report here crystal structures of the binary, complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or, N-acetyl-L-ornithine (AORN), and the ternary complex with CP and, N-acetyl-L-norvaline. Comparison of these structures demonstrates that the, substrate-binding mechanism of this novel transcarbamoylase is different, from those of aspartate and ornithine transcarbamoylases, both of which, show ordered substrate binding with large domain movements. CP and AORN, bind to AOTCase independently, and the main conformational change upon, substrate binding is ordering of the 80's loop, with a small domain, closure around the active site and little movement of the 240's loop. The, structures of the complexes provide insight into the mode of substrate, binding and the mechanism of the transcarbamoylation reaction.
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| - | ==About this Structure==
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| - | 1ZQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris] with SO4, AOR and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZQ6 OCA].
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| - | ==Reference==
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| - | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis., Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM, Proteins. 2006 Aug 1;64(2):532-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16741992 16741992]
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| - | [[Category: Ornithine carbamoyltransferase]]
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| - | [[Category: Single protein]]
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| - | [[Category: Xanthomonas campestris]]
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| - | [[Category: Allewell, N.M.]]
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| - | [[Category: Malamy, M.H.]]
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| - | [[Category: Morizono, H.]]
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| - | [[Category: Roth, L.]]
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| - | [[Category: Shi, D.]]
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| - | [[Category: Tuchman, M.]]
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| - | [[Category: Yu, X.]]
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| - | [[Category: AOR]]
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| - | [[Category: GOL]]
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| - | [[Category: SO4]]
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| - | [[Category: alpha/beta two-domain]]
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:36:02 2007''
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