| RRC ID |
35225
|
| Author |
Krieg S, Huché F, Diederichs K, Izadi-Pruneyre N, Lecroisey A, Wandersman C, Delepelaire P, Welte W.
|
| Title |
Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.
|
| Journal |
Proc Natl Acad Sci U S A
|
| Abstract |
Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores) to scavenge and actively transport heme. To unravel the unknown molecular details involved, we present 3 structures of the Serratia marcescens receptor HasR in complex with its hemophore HasA. The transfer of heme over a distance of 9 A from its high-affinity site in HasA into a site of lower affinity in HasR is coupled with the exergonic complex formation of the 2 proteins. Upon docking to the receptor, 1 of the 2 axial heme coordinations of the hemophore is initially broken, but the position and orientation of the heme is preserved. Subsequently, steric displacement of heme by a receptor residue ruptures the other axial coordination, leading to heme transfer into the receptor.
|
| Volume |
106(4)
|
| Pages |
1045-50
|
| Published |
2009-1-27
|
| DOI |
10.1073/pnas.0809406106
|
| PII |
0809406106
|
| PMID |
19144921
|
| PMC |
PMC2633585
|
| MeSH |
Apoproteins / chemistry
Apoproteins / metabolism
Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism
Biological Transport
Calorimetry
Carrier Proteins / chemistry*
Carrier Proteins / metabolism
Cell Membrane / metabolism*
Crystallography, X-Ray
Heme / chemistry
Heme / metabolism*
Heme-Binding Proteins
Hemeproteins / chemistry*
Hemeproteins / metabolism
Ligands
Membrane Proteins / chemistry*
Membrane Proteins / metabolism
Models, Molecular
Protein Structure, Secondary
Receptors, Cell Surface / chemistry*
Receptors, Cell Surface / metabolism
Serratia marcescens / chemistry*
Surface Properties
|
| IF |
9.412
|
| Times Cited |
110
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Prokaryotes E. coli |
|
