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| | <StructureSection load='2c7t' size='340' side='right'caption='[[2c7t]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2c7t' size='340' side='right'caption='[[2c7t]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_24 Atcc 24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C7T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c81|2c81]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2c7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7t OCA], [https://pdbe.org/2c7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7t RCSB], [https://www.ebi.ac.uk/pdbsum/2c7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7t 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=2c7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7t OCA], [https://pdbe.org/2c7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c7t RCSB], [https://www.ebi.ac.uk/pdbsum/2c7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLDSA_BACCI GLDSA_BACCI]] Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (DOI) to form 2-deoxy-scyllo-inosamine (DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI) into 2-deoxystreptamine (DOS). Is also able to catalyze the transamination of scyllo-inosose to form scyllo-inosamine, although this reaction may be not physiological.<ref>PMID:12374384</ref> <ref>PMID:12478783</ref> <ref>PMID:15839685</ref>
| + | [https://www.uniprot.org/uniprot/GLDSA_NIACI GLDSA_NIACI] Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine (2-DOS).<ref>PMID:12374384</ref> <ref>PMID:12478783</ref> <ref>PMID:15839685</ref> |
| | == 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: Atcc 24]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blundell, T L]] | + | [[Category: Niallia circulans]] |
| - | [[Category: Chirgadze, D Y]] | + | [[Category: Blundell TL]] |
| - | [[Category: Huang, F]] | + | [[Category: Chirgadze DY]] |
| - | [[Category: Popovic, B]] | + | [[Category: Huang F]] |
| - | [[Category: Spencer, J B]] | + | [[Category: Popovic B]] |
| - | [[Category: Tang, X]] | + | [[Category: Spencer JB]] |
| - | [[Category: Aminoglycoside antibiotic]]
| + | [[Category: Tang X]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Butirosin]]
| + | |
| - | [[Category: Smat]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLDSA_NIACI Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine (2-DOS).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.
Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.,Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tamegai H, Nango E, Kuwahara M, Yamamoto H, Ota Y, Kuriki H, Eguchi T, Kakinuma K. Identification of L-glutamine: 2-deoxy-scyllo-inosose aminotransferase required for the biosynthesis of butirosin in Bacillus circulans. J Antibiot (Tokyo). 2002 Aug;55(8):707-14. PMID:12374384
- ↑ Huang F, Li Y, Yu J, Spencer JB. Biosynthesis of aminoglycoside antibiotics: cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine. Chem Commun (Camb). 2002 Dec 7;(23):2860-1. PMID:12478783
- ↑ Yokoyama K, Kudo F, Kuwahara M, Inomata K, Tamegai H, Eguchi T, Kakinuma K. Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis. J Am Chem Soc. 2005 Apr 27;127(16):5869-74. PMID:15839685 doi:http://dx.doi.org/10.1021/ja0445948
- ↑ Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB. Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis. Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611 doi:10.1002/prot.21076
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