1iu9: Difference between revisions
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<StructureSection load='1iu9' size='340' side='right'caption='[[1iu9]], [[Resolution|resolution]] 2.04Å' scene=''> | <StructureSection load='1iu9' size='340' side='right'caption='[[1iu9]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iu9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1iu9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IU9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iu9 OCA], [https://pdbe.org/1iu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iu9 RCSB], [https://www.ebi.ac.uk/pdbsum/1iu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iu9 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/RACD_PYRHO RACD_PYRHO] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii OT3]] | ||
[[Category: Iwata | [[Category: Iwata K]] | ||
[[Category: Liu | [[Category: Liu L]] | ||
[[Category: Miki | [[Category: Miki K]] | ||
[[Category: Yohda | [[Category: Yohda M]] | ||
Revision as of 02:37, 28 December 2023
Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases.,Liu L, Iwata K, Yohda M, Miki K FEBS Lett. 2002 Sep 25;528(1-3):114-8. PMID:12297289[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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