Gramicidin

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[[Image:2xdc.png|left|200px|thumb|Crystal Structure of Gramicidin, [[2xdc]]]]
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<StructureSection load='1gmk' size='350' side='right' caption='Gramicidin A complex with thiocyanate and K+ ion (purple) (PDB entry [[1gmk]])' scene='44/444642/Cv/2'>
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<Structure load='1al4' size='400' scene= frame='true' align='right' caption='Gramicidin D dimer with formyl-valine, formyl-isoleucine complex with propanol and ethanolamine , [[1al4]]'/>
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== Function ==
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[[Gramicidin]] (GCDN) is a polypeptide composed of alternating L- and D-amino acids. It is produced by the bacteria ''Bacillus brevis''<ref>PMID:5288776</ref>.<br />
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* '''GCDN S''' is an antibiotic cyclic polypeptide.<br />
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* '''GCDN D''' is a mixture of GCDN A, B, C. <br />
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See theoretical model of [[Gramicidin Channel in Lipid Bilayer]] and [[Gramicidin Channel in Lipid Bilayer (Spanish)]].
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==Relevance ==
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GCDN has bactericidal activity and is used as a topical antibiotic and as topical contraceptive<ref>PMID:8836773</ref>.
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== Structural highlights: Gramicidin A==
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Protein:
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<scene name='44/444642/Cv/7'>Chains</scene>, chain A in green, chain B in salmon.
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Non-standard residues:
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<scene name='44/444642/Cv/8'>Ethanloamine</scene>
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<scene name='44/444642/Cv/9'>D-leucine</scene>
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<scene name='44/444642/Cv/10'>D-valine</scene>
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<scene name='44/444642/Cv/11'>N-formyl-L-valine</scene>
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Ligands:
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<scene name='44/444642/Cv/4'>Methanol</scene>, C atom of methanol in cyan.
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<scene name='44/444642/Cv/5'>Thiocyanate</scene>, C atom of thiocyanate in magenta.
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<scene name='44/444642/Cv/6'>K+ ion</scene> (in purple).
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</StructureSection>
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[[Gramicidin]] (GCDN) is a polypeptide composed of alternating L- and D-amino acids. It has bactericidal activity and is used as antibiotic. It is produced by the bacteria ''Bacillus brevis''. GCDN S is a cyclic polypeptide. GCDN D is a mixture of GCDN A, B, C.
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GCDN S is an antibiotic. See theoretical model of [[Gramicidin Channel in Lipid Bilayer]].
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{{TOC limit|limit=2}}
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== 3D Structures of Gramicidin ==
== 3D Structures of Gramicidin ==
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''Update February 2013''
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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===Gramicidin A===
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[[1nt5]], [[1nt6]], [[1nrm]], [[1nru]], [[1ng8]], [[1kqe]], [[1jno]], [[1jo3]], [[1jo4]], [[1mic]], [[1mag]], [[1grm]] - GCDN A – NMR<br />
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*Gramicidin A
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[[1tkq]] - GCDN A + mini-GCDN A – NMR<br />
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[[1av2]] - GCDN A + CsCl<br />
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[[1gmk]] - GCDN A + KCNS
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===Gramicidin D===
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**[[1nt5]], [[1nt6]], [[1nrm]], [[1nru]], [[1ng8]], [[1kqe]], [[1jno]], [[1jo3]], [[1jo4]], [[1mic]], [[1mag]], [[1grm]] - GCDN A – NMR<br />
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**[[1tkq]] - GCDN A + mini-GCDN A – NMR<br />
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**[[1av2]] - GCDN A + CsCl<br />
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**[[1gmk]] - GCDN A + KCNS
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[[2xdc]], [[1w5u]], [[1bdw]], [[1al4]], [[1alx]], [[1alz]], [[2y5m]], [[2y6n]] – GCDN D<br />
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*Gramicidin D
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[[3lml]], [[2izq]], [[3i8i]], [[3l8l]] - GCDN D + iodide<br />
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[[1c4d]] - GCDN D + CsCl<br />
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[[3zq8]] – GCDN D + monovaccenin
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===Gramicidin S===
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**[[2xdc]], [[1w5u]], [[1bdw]], [[1al4]], [[1alx]], [[1alz]], [[2y5m]], [[2y6n]] – GCDN D<br />
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**[[3lml]], [[2izq]], [[4v6f]], [[3l8l]] - GCDN D + iodide<br />
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**[[1c4d]] - GCDN D + CsCl<br />
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**[[3zq8]] – GCDN D + monovaccenin
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[[1tk2]] – GCDN S + subtilisin savinase – ''Bacillus lentus''
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*Gramicidin S
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**[[1tk2]] – GCDN S + subtilisin savinase – ''Bacillus lentus''
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**[[8rc7]] – GCDN S + urea<br />
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}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Gramicidin A complex with thiocyanate and K+ ion (purple) (PDB entry 1gmk)

Drag the structure with the mouse to rotate

3D Structures of Gramicidin

Updated on 27-July-2025

References

  1. ↑ Urry DW, Goodall MC, Glickson JD, Mayers DF. The gramicidin A transmembrane channel: characteristics of head-to-head dimerized (L,D) helices. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1907-11. PMID:5288776
  2. ↑ Kondejewski LH, Farmer SW, Wishart DS, Hancock RE, Hodges RS. Gramicidin S is active against both gram-positive and gram-negative bacteria. Int J Pept Protein Res. 1996 Jun;47(6):460-6. PMID:8836773

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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