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| <StructureSection load='6l8p' size='340' side='right'caption='[[6l8p]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6l8p' size='340' side='right'caption='[[6l8p]], [[Resolution|resolution]] 1.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6l8p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Psychrobacter_sp._mes7-p7e Psychrobacter sp. mes7-p7e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L8P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6l8p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Psychrobacter_sp._MES7-P7E Psychrobacter sp. MES7-P7E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L8P FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.601Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CXF62_02540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2058322 Psychrobacter sp. MES7-P7E])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6l8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8p OCA], [http://pdbe.org/6l8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l8p RCSB], [http://www.ebi.ac.uk/pdbsum/6l8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8p ProSAT]</span></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=6l8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8p OCA], [https://pdbe.org/6l8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l8p RCSB], [https://www.ebi.ac.uk/pdbsum/6l8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8p ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A0A2N5LLK3_9GAMM A0A2N5LLK3_9GAMM] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Psychrobacter sp. mes7-p7e]] | + | [[Category: Psychrobacter sp. MES7-P7E]] |
- | [[Category: Koh, H Y]] | + | [[Category: Koh HY]] |
- | [[Category: Kwon, S]] | + | [[Category: Kwon S]] |
- | [[Category: Lee, C W]] | + | [[Category: Lee CW]] |
- | [[Category: Lee, J H]] | + | [[Category: Lee JH]] |
- | [[Category: Park, H H]] | + | [[Category: Park HH]] |
- | [[Category: Antarctic bacterium]]
| + | |
- | [[Category: Cold-adaptability]]
| + | |
- | [[Category: Deamination]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Psychrophile]]
| + | |
- | [[Category: Rida]]
| + | |
| Structural highlights
Function
A0A2N5LLK3_9GAMM
Publication Abstract from PubMed
The RidA subfamily proteins catalyze the deamination reaction of enamine/imine intermediates, which are metabolites of amino acids such as threonine and serine. Numerous structural and functional studies have been conducted on RidA isolated from mesophiles and thermophiles. However, little is known about the structure of the RidA proteins isolated from psychrophiles. In the present study, we elucidated the crystal structure of RidA from the Antarctic bacterium Psychrobacter sp. PAMC 21119 (Pp-RidA) at 1.6 A resolution to identify the structural properties contributing to cold-adaptability. Although the overall structure of Pp-RidA is similar to those of its homologues, it exhibits specific structural arrangements of a loop positioned near the active site, which is assumed to play a role in covering the active site of catalysis. In addition, the surface electrostatic potential of Pp-RidA suggested that it exhibits stronger electrostatic distribution relative to its homologues. Our results provide novel insights into the key determinants of cold-adaptability.
Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119.,Kwon S, Lee CW, Koh HY, Park H, Lee JH, Park HH Biochem Biophys Res Commun. 2019 Nov 27. pii: S0006-291X(19)32267-3. doi:, 10.1016/j.bbrc.2019.11.139. PMID:31785813[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kwon S, Lee CW, Koh HY, Park H, Lee JH, Park HH. Crystal structure of the reactive intermediate/imine deaminase A homolog from the Antarctic bacterium Psychrobacter sp. PAMC 21119. Biochem Biophys Res Commun. 2019 Nov 27. pii: S0006-291X(19)32267-3. doi:, 10.1016/j.bbrc.2019.11.139. PMID:31785813 doi:http://dx.doi.org/10.1016/j.bbrc.2019.11.139
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