1iu9: Difference between revisions

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-[[Image:1iu9.jpg|left|200px]]<br /><applet load="1iu9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1iu9.jpg|left|200px]]<br /><applet load="1iu9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1iu9, resolution 2.04&Aring;" />
 '''Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3'''<br />
 ==Overview==
-The X-ray crystal structure has revealed two similar alpha/beta domains of, aspartate racemase (AspR) from Pyrococcus horikoshii OT3, and identified a, pseudo mirror-symmetric distribution of the residues around its active, site [Liu et al. (2002) J. Mol. Biol. 319, 479-489]. Structural homology, and functional similarity between the two domains suggested that this, enzyme evolved from an ancestral domain by gene duplication and gene, fusion. We have expressed solely the C-terminal domain of this AspR and, determined its three-dimensional structure by X-ray crystallography. The, high structural stability of this domain supports the existence of the, ancestral domain. In comparison with other amino acid racemases (AARs), we, suggest that gene duplication and gene fusion are conventional ways in the, evolution of pyridoxal 5'-phosphate-independent AARs.
+The X-ray crystal structure has revealed two similar alpha/beta domains of aspartate racemase (AspR) from Pyrococcus horikoshii OT3, and identified a pseudo mirror-symmetric distribution of the residues around its active site [Liu et al. (2002) J. Mol. Biol. 319, 479-489]. Structural homology and functional similarity between the two domains suggested that this enzyme evolved from an ancestral domain by gene duplication and gene fusion. We have expressed solely the C-terminal domain of this AspR and determined its three-dimensional structure by X-ray crystallography. The high structural stability of this domain supports the existence of the ancestral domain. In comparison with other amino acid racemases (AARs), we suggest that gene duplication and gene fusion are conventional ways in the evolution of pyridoxal 5'-phosphate-independent AARs.
 ==About this Structure==
-IU9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate_racemase Aspartate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.13 5.1.1.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IU9 OCA].
+IU9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate_racemase Aspartate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.13 5.1.1.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU9 OCA].
 ==Reference==
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 [[Category: crystal structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:32:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:44 2008''