2ip6
From Proteopedia
(New page: 200px<br /><applet load="2ip6" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ip6, resolution 1.35Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | BACKGROUND: Pediocin-like bacteriocins, ribosomally-synthesized | + | BACKGROUND: Pediocin-like bacteriocins, ribosomally-synthesized antimicrobial peptides, are generally coexpressed with cognate immunity proteins in order to protect the bacteriocin-producer from its own bacteriocin. As a step for understanding the mode of action of immunity proteins, we determined the crystal structure of PedB, a pediocin-like immunity protein conferring immunity to pediocin PP-1. RESULTS: The 1.6 A crystal structure of PedB reveals that PedB consists of an antiparallel four-helix bundle with a flexible C-terminal end. PedB shows structural similarity to an immunity protein against enterocin A (EntA-im) but some disparity to an immunity protein against carnobacteriocin B2 (ImB2) in both the C-terminal conformation and the local structure constructed by alpha3, alpha4, and their connecting loop. Structure-inspired mutational studies reveal that deletion of the last seven residues of the C-terminus of PedB almost abolished its immunity activity. CONCLUSION: The fact that PedB, EntA-im, and ImB2 share a four-helix bundle structure strongly suggests the structural conservation of this motif in the pediocin-like immunity proteins. The significant difference in the core structure and the C-terminal conformation provides a structural basis for the classification of pediocin-like immunity proteins. Our mutational study using C-terminal-shortened PedBs and the investigation of primary sequence of the C-terminal region, propose that several polar or charged residues in the extreme C-terminus of PedB which is crucial for the immunity are involved in the specific recognition of pediocin PP-1. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pediococcus pentosaceus]] | [[Category: Pediococcus pentosaceus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cha, S | + | [[Category: Cha, S S.]] |
| - | [[Category: Kang, S | + | [[Category: Kang, S O.]] |
| - | [[Category: Kim, I | + | [[Category: Kim, I K.]] |
| - | [[Category: Kim, J | + | [[Category: Kim, J H.]] |
| - | [[Category: Kim, M | + | [[Category: Kim, M K.]] |
| - | [[Category: Yim, H | + | [[Category: Yim, H S.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: antimicrobial protein]] | [[Category: antimicrobial protein]] | ||
[[Category: immunity protein to the pediocin pp-1]] | [[Category: immunity protein to the pediocin pp-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:49 2008'' |
Revision as of 15:54, 21 February 2008
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Crystal structure of PedB
Overview
BACKGROUND: Pediocin-like bacteriocins, ribosomally-synthesized antimicrobial peptides, are generally coexpressed with cognate immunity proteins in order to protect the bacteriocin-producer from its own bacteriocin. As a step for understanding the mode of action of immunity proteins, we determined the crystal structure of PedB, a pediocin-like immunity protein conferring immunity to pediocin PP-1. RESULTS: The 1.6 A crystal structure of PedB reveals that PedB consists of an antiparallel four-helix bundle with a flexible C-terminal end. PedB shows structural similarity to an immunity protein against enterocin A (EntA-im) but some disparity to an immunity protein against carnobacteriocin B2 (ImB2) in both the C-terminal conformation and the local structure constructed by alpha3, alpha4, and their connecting loop. Structure-inspired mutational studies reveal that deletion of the last seven residues of the C-terminus of PedB almost abolished its immunity activity. CONCLUSION: The fact that PedB, EntA-im, and ImB2 share a four-helix bundle structure strongly suggests the structural conservation of this motif in the pediocin-like immunity proteins. The significant difference in the core structure and the C-terminal conformation provides a structural basis for the classification of pediocin-like immunity proteins. Our mutational study using C-terminal-shortened PedBs and the investigation of primary sequence of the C-terminal region, propose that several polar or charged residues in the extreme C-terminus of PedB which is crucial for the immunity are involved in the specific recognition of pediocin PP-1.
About this Structure
2IP6 is a Single protein structure of sequence from Pediococcus pentosaceus with as ligand. Full crystallographic information is available from OCA.
Reference
High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins., Kim IK, Kim MK, Kim JH, Yim HS, Cha SS, Kang SO, BMC Struct Biol. 2007 May 30;7:35. PMID:17537233
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