This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3ftj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 21:52, 25 December 2014

Crystal structure of the periplasmic region of MacB from Actinobacillus actinomycetemcomitans

Structural highlights

3ftj is a 1 chain structure with sequence from Aggregatibacter actinomycetemcomitans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	macB, MACB_ACTAC (Aggregatibacter actinomycetemcomitans)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MACB_ACTAC] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720]

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

MacB is a noncanonic ABC-type transporter within Gram-negative bacteria, which is responsible both for the efflux of macrolide antibiotics and for the secretion of heat-stable enterotoxin II. In Escherichia coli, MacB requires the membrane fusion protein MacA and the multifunctional outer membrane channel TolC to pump substrates to the external medium. Sequence analysis of MacB suggested that MacB has a relatively large periplasmic region. To gain insight into how MacB assembles with MacA and TolC, we determined the crystal structure of the periplasmic region of Actinobacillus actinomycetemcomitans MacB. Fold matching program reveals that parts of the MacB periplasmic region have structural motifs in common with the RND-type transporter AcrB. Since it behaved as a monomer in solution, our finding is consistent with the dimeric nature of full-length MacB, providing an insight into the assembly in the tripartite efflux pump.

Crystal Structure of the Periplasmic Region of MacB, a Noncanonic ABC Transporter (,).,Xu Y, Sim SH, Nam KH, Jin XL, Kim HM, Hwang KY, Lee K, Ha NC Biochemistry. 2009 May 21. PMID:19432486^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xu Y, Sim SH, Nam KH, Jin XL, Kim HM, Hwang KY, Lee K, Ha NC. Crystal Structure of the Periplasmic Region of MacB, a Noncanonic ABC Transporter (,). Biochemistry. 2009 May 21. PMID:19432486 doi:10.1021/bi900415t

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ftj"

@@ Line 6: / Line 6: @@
 <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=3ftj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ftj RCSB], [http://www.ebi.ac.uk/pdbsum/3ftj PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MACB_ACTAC MACB_ACTAC]] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3ftj

From Proteopedia

Revision as of 21:52, 25 December 2014

Crystal structure of the periplasmic region of MacB from Actinobacillus actinomycetemcomitans

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox