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== | ==INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUS== | ||
<StructureSection load='1bwd' size='340' side='right'caption='[[1bwd]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[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/bw/1bwd_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=1bwd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | 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<ref>PMID:9922132</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1bwd" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Streptomyces | <references/> | ||
[[Category: Bergner | __TOC__ | ||
[[Category: Fritsche | </StructureSection> | ||
[[Category: Huber | [[Category: Large Structures]] | ||
[[Category: Humm | [[Category: Streptomyces griseus]] | ||
[[Category: Piepersberg | [[Category: Bergner A]] | ||
[[Category: Fritsche E]] | |||
[[Category: Huber R]] | |||
[[Category: Humm A]] | |||
[[Category: Piepersberg W]] | |||
Latest revision as of 08:44, 9 August 2023
INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUSINOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUS
Structural highlights
FunctionSTRB1_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 PubMedInosamine-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 |
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