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| | <StructureSection load='1bwd' size='340' side='right'caption='[[1bwd]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='1bwd' size='340' side='right'caption='[[1bwd]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BWD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STRB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 "Actinomyces griseus" Krainsky 1914])</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]] 3.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Scyllo-inosamine-4-phosphate_amidinotransferase Scyllo-inosamine-4-phosphate amidinotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.4.2 2.1.4.2] </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=1bwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwd OCA], [https://pdbe.org/1bwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwd RCSB], [https://www.ebi.ac.uk/pdbsum/1bwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwd ProSAT]</span></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=1bwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwd OCA], [http://pdbe.org/1bwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bwd RCSB], [http://www.ebi.ac.uk/pdbsum/1bwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STRB1_STRGR STRB1_STRGR]] Catalyzes two non-consecutive transamidination reactions. It converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine 4-phosphate and N1-amidinostreptamine 6-phosphate into streptidine 6-phosphate. | + | [https://www.uniprot.org/uniprot/STRB1_STRGR STRB1_STRGR] Catalyzes two non-consecutive transamidination reactions. It converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine 4-phosphate and N1-amidinostreptamine 6-phosphate into streptidine 6-phosphate. |
| | == 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: Actinomyces griseus krainsky 1914]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Scyllo-inosamine-4-phosphate amidinotransferase]] | + | [[Category: Streptomyces griseus]] |
| - | [[Category: Bergner, A]] | + | [[Category: Bergner A]] |
| - | [[Category: Fritsche, E]] | + | [[Category: Fritsche E]] |
| - | [[Category: Huber, R]] | + | [[Category: Huber R]] |
| - | [[Category: Humm, A]] | + | [[Category: Humm A]] |
| - | [[Category: Piepersberg, W]] | + | [[Category: Piepersberg W]] |
| - | [[Category: Amidinotransferase]]
| + | |
| - | [[Category: Streptomycin]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
STRB1_STRGR Catalyzes two non-consecutive transamidination reactions. It converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine 4-phosphate and N1-amidinostreptamine 6-phosphate into streptidine 6-phosphate.
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
Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. L-Arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) was cloned as an N-terminal hexa-histidine fusion protein, purified by affinity chromatography, and crystallized, and its crystal structure was solved by Patterson search methods at 3.1 A resolution. The structure is composed of five betabeta alphabeta-modules which are arranged circularly into a pseudo-5-fold symmetric particle. The three-dimensional structure is closely related to the structure of human L-arginine:glycine amidinotransferase (AT), but five loops (the 40-, 170-, 220-, 250-, and 270-loop) are organized very differently. The major changes are found in loops around the active site which open the narrow active site channel of AT to form an open and solvent-exposed cavity. In particular, module II of StrB1 is AT-like but lacks a 10-residue alpha-helix in the 170-loop. The concomitant reorganization of neighboring surface loops that surround the active site, i.e., the 40-loop and the 270-loop, results in an arrangement of loops which allows an unrestricted access of substrates to the cavity. However, the residues which are involved in substrate binding and catalysis are conserved in AT and StrB1 and are at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases. The binding site for L-arginine had been deduced from its complex with AT. Molecular modeling revealed a possible binding mode for the second substrate scyllo-inosamine 4-phosphate.
Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis.,Fritsche E, Bergner A, Humm A, Piepersberg W, Huber R Biochemistry. 1998 Dec 22;37(51):17664-72. PMID:9922132[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fritsche E, Bergner A, Humm A, Piepersberg W, Huber R. Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis. Biochemistry. 1998 Dec 22;37(51):17664-72. PMID:9922132
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