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.

1ybj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structural and Dynamics studies of both apo and holo forms of the hemophore HasA

Structural highlights

1ybj is a 1 chain structure with sequence from Serratia marcescens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HASA_SERMA Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.^[1] ^[2]

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

A heme-acquisition system present in several Gram-negative bacteria requires the secretion of hemophores. These extracellular carrier proteins capture heme and deliver it to specific outer membrane receptors. The Serratia marcescens HasA hemophore is a monodomain protein that binds heme with a very high affinity. Its alpha/beta structure, as that of its binding pocket, has no common features with other iron- or heme-binding proteins. Heme is held by two loops L1 and L2 and coordinated to iron by an unusual ligand pair, H32/Y75. Two independent regions of the hemophore beta-sheet are involved in HasA-HasR receptor interaction. Here, we report the 3-D NMR structure of apoHasA and the backbone dynamics of both loaded and unloaded hemophore. While the overall structure of HasA is very similar in the apo and holo forms, the hemophore presents a transition from an open to a closed form upon ligand binding, through a large movement, of up to 30 A, of loop L1 bearing H32. Comparison of loaded and unloaded HasA dynamics on different time scales reveals striking flexibility changes in the binding pocket. We propose a mechanism by which these structural and dynamic features provide the dual function of heme binding and release to the HasR receptor.

Comparative analysis of structural and dynamic properties of the loaded and unloaded hemophore HasA: functional implications.,Wolff N, Izadi-Pruneyre N, Couprie J, Habeck M, Linge J, Rieping W, Wandersman C, Nilges M, Delepierre M, Lecroisey A J Mol Biol. 2008 Feb 15;376(2):517-25. Epub 2007 Dec 4. PMID:18164722^[3]

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

References

↑ Letoffe S, Ghigo JM, Wandersman C. Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9876-80. PMID:7937909
↑ Ghigo JM, Letoffe S, Wandersman C. A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J Bacteriol. 1997 Jun;179(11):3572-9. PMID:9171402
↑ Wolff N, Izadi-Pruneyre N, Couprie J, Habeck M, Linge J, Rieping W, Wandersman C, Nilges M, Delepierre M, Lecroisey A. Comparative analysis of structural and dynamic properties of the loaded and unloaded hemophore HasA: functional implications. J Mol Biol. 2008 Feb 15;376(2):517-25. Epub 2007 Dec 4. PMID:18164722 doi:10.1016/j.jmb.2007.11.072

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/1ybj"

@@ Line 1: / Line 1: @@
 ==Structural and Dynamics studies of both apo and holo forms of the hemophore HasA==
-<StructureSection load='1ybj' size='340' side='right'caption='[[1ybj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1ybj' size='340' side='right'caption='[[1ybj]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ybj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YBJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ybj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YBJ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hasA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=615 "Bacillus marcescens" (Bizio 1823) Trevisan in de Toni and Trevisan 1889])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ybj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybj OCA], [https://pdbe.org/1ybj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ybj RCSB], [https://www.ebi.ac.uk/pdbsum/1ybj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ybj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HASA_SERMA HASA_SERMA]] Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.<ref>PMID:7937909</ref> <ref>PMID:9171402</ref>
+[https://www.uniprot.org/uniprot/HASA_SERMA HASA_SERMA] Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.<ref>PMID:7937909</ref> <ref>PMID:9171402</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Couprie, J]]
+[[Category: Serratia marcescens]]
-[[Category: Delepierre, M]]
+[[Category: Couprie J]]
-[[Category: Habeck, M]]
+[[Category: Delepierre M]]
-[[Category: Izadi-Pruneyre, N]]
+[[Category: Habeck M]]
-[[Category: Lecroisey, A]]
+[[Category: Izadi-Pruneyre N]]
-[[Category: Linge, J]]
+[[Category: Lecroisey A]]
-[[Category: Nilges, M]]
+[[Category: Linge J]]
-[[Category: Rieping, W]]
+[[Category: Nilges M]]
-[[Category: Wandersman, C]]
+[[Category: Rieping W]]
-[[Category: Wolff, N]]
+[[Category: Wandersman C]]
-[[Category: Alpha+beta structure]]
+[[Category: Wolff N]]
-[[Category: Curved anti-parallel beta-sheet]]
-[[Category: Metal binding protein]]

1ybj

From Proteopedia

Current revision

Structural and Dynamics studies of both apo and holo forms of the hemophore HasA

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