Linear gramicidin synthase
From Proteopedia
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'''Linear gramicidin synthase''' LgrA is a biosynthetic enzyme which synthesizes natural products for therapeutics using a modular synthetic logic where each module adds one amino acid to the growing chain. | '''Linear gramicidin synthase''' LgrA is a biosynthetic enzyme which synthesizes natural products for therapeutics using a modular synthetic logic where each module adds one amino acid to the growing chain. | ||
| - | Thus, LgrA is a non-ribosomal peptide synthetase<ref>PMID:31699907</ref>. | + | Thus, LgrA is a non-ribosomal peptide synthetase<ref>PMID:31699907</ref>. Linear gramicidin is a 15 amino acid long polypeptide which is synthetized by synthases LgrA, LgrB, LgrC, LgrD which comprise 16 modules<ref>PMID:15938641</ref>. |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| + | LgrA core contains 3 essential domains. Adenylation domain which activates the specific amino acid aby adenylation, the thiolation domain which produces a thiol ester and the condensation domain which catalyzes the elongation of the peptide chain. | ||
</StructureSection> | </StructureSection> | ||
| + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
==3D structures of linear gramicidin synthase subunit A== | ==3D structures of linear gramicidin synthase subunit A== | ||
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== References == | == References == | ||
<references/> | <references/> | ||
| + | [[Category:Topic Page]] | ||
Revision as of 07:56, 4 October 2020
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Updated on 04-October-2020
3D structures of linear gramicidin synthase subunit A
5jnf, 5es6 - BpLgrA 2 domains 2-584 - Brevibacillus parabrevis
6ulz - BpLgrA adenylation domain (mutant) 2-684
5es7 - BpLgrA adenylation domain 2-684 + Val + APC + FON
5es5, 5es8, 5es9 - BpLgrA initiation domain 2-766
6mfw - BpLgrA 4 domains 2-1198
6mfx - BpLgrA 4 domains (mutant) 2-1198
6mfy, 6mg0 - BpLgrA 5 domains 2-1716
6mfz - BpLgrA 2-1802
References
- ↑ Reimer JM, Eivaskhani M, Harb I, Guarne A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility. Science. 2019 Nov 8;366(6466). pii: 366/6466/eaaw4388. doi:, 10.1126/science.aaw4388. PMID:31699907 doi:http://dx.doi.org/10.1126/science.aaw4388
- ↑ Schracke N, Linne U, Mahlert C, Marahiel MA. Synthesis of linear gramicidin requires the cooperation of two independent reductases. Biochemistry. 2005 Jun 14;44(23):8507-13. PMID:15938641 doi:http://dx.doi.org/10.1021/bi050074t
