1r0m
From Proteopedia
(Difference between revisions)
m (Protected "1r0m" [edit=sysop:move=sysop]) |
|||
(7 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:1r0m.png|left|200px]] | ||
- | + | ==Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity== | |
- | + | <StructureSection load='1r0m' size='340' side='right'caption='[[1r0m]], [[Resolution|resolution]] 1.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1r0m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R0M FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</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=1r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0m OCA], [https://pdbe.org/1r0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r0m RCSB], [https://www.ebi.ac.uk/pdbsum/1r0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0m ProSAT]</span></td></tr> | |
- | == | + | </table> |
- | [[1r0m]] is a 4 chain structure with sequence from [ | + | == Function == |
- | + | [https://www.uniprot.org/uniprot/NSAR_DEIRA NSAR_DEIRA] Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-L-phenylglycine and N-succinyl-D/L-phenylalanine (PubMed:24872444, PubMed:25875730). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-acetyl-D/L-phenylalanine, N-acetyl-L-glutamine, N-acetyl-L-tryptophan, N-acetyl-L-leucine, N-formyl-D-methionine, N-formyl-D-norleucine, N-carbamoyl-D-methionine and N-carbamoyl-D-norleucine (PubMed:15313614, PubMed:16650857, PubMed:25875730). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:24872444). However, NSAR activity is probably the protein's biological function, because menaquinone biosynthesis genes are missing in this species (Probable).<ref>PMID:15313614</ref> <ref>PMID:16650857</ref> <ref>PMID:24872444</ref> <ref>PMID:25875730</ref> <ref>PMID:16740275</ref> | |
- | == | + | == Evolutionary Conservation == |
- | < | + | [[Image:Consurf_key_small.gif|200px|right]] |
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/1r0m_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r0m ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
- | [[Category: Chen | + | [[Category: Large Structures]] |
- | [[Category: Chiu | + | [[Category: Chen C-Y]] |
- | [[Category: Hsu | + | [[Category: Chiu W-C]] |
- | [[Category: Hsu | + | [[Category: Hsu S-K]] |
- | [[Category: Liu | + | [[Category: Hsu W-H]] |
- | [[Category: Wang | + | [[Category: Liu J-S]] |
- | [[Category: Wu | + | [[Category: Wang W-C]] |
- | + | [[Category: Wu C-L]] | |
- | + |
Current revision
Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity
|
Categories: Deinococcus radiodurans | Large Structures | Chen C-Y | Chiu W-C | Hsu S-K | Hsu W-H | Liu J-S | Wang W-C | Wu C-L