4myp

From Proteopedia

(Difference between revisions)

Revision as of 10:20, 28 December 2022

Structure of the central NEAT domain, N2, of the listerial Hbp2 protein complexed with heme

Structural highlights

4myp is a 2 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBP2_LISMO Acts as an extracellular and cell wall-bound hemophore; scavenges host heme and hemoglobin from the environment and also serves as a cell wall receptor for both (Probable). At low hemin (Hn) and hemoglobin (Hb) concentrations adsorbs Hn/Hb and presumably directs it to membrane transporters (Probable). Soluble Hbp2 can probably pass Hn/Hb to cell wall-anchored Hbp2, and both forms can accept Hn/Hb from Hbp1 (PubMed:25315777). May be involved in crossing the digestive barrier in infected animals (PubMed:15661014). Binds host hemin (Probable) (PubMed:21545655, PubMed:25315777). Binds host hemoglobin with affinity in the nanomolar range (PubMed:25315777).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Iron is an essential nutrient that is required for the growth of the bacterial pathogen Listeria monocytogenes. In cell cultures, this microbe secretes hemin/hemoglobin-binding protein 2 (Hbp2; Lmo2185) protein, which has been proposed to function as a hemophore that scavenges heme from the environment. Based on its primary sequence, Hbp2 contains three NEAr transporter (NEAT) domains of unknown function. Here we show that each of these domains mediates high affinity binding to ferric heme (hemin) and that its N- and C-terminal domains interact with hemoglobin (Hb). The results of hemin transfer experiments are consistent with Hbp2 functioning as an Hb-binding hemophore that delivers hemin to other Hbp2 proteins that are attached to the cell wall. Surprisingly, our work reveals that the central NEAT domain in Hbp2 binds hemin even though its primary sequence lacks a highly conserved YXXXY motif that is used by all other previously characterized NEAT domains to coordinate iron in the hemin molecule. To elucidate the mechanism of hemin binding by Hbp2, we determined crystal structures of its central NEAT domain (Hbp2(N2); residues 183-303) in its free and hemin-bound states. The structures reveal an unprecedented mechanism of hemin binding in which Hbp2(N2) undergoes a major conformational rearrangement that facilitates metal coordination by a non-canonical tyrosine residue. These studies highlight previously unrecognized plasticity in the hemin binding mechanism of NEAT domains and provide insight into how L. monocytogenes captures heme iron.

Novel Mechanism of Hemin Capture by Hbp2, the Hemoglobin-binding Hemophore from Listeria monocytogenes.,Malmirchegini GR, Sjodt M, Shnitkind S, Sawaya MR, Rosinski J, Newton SM, Klebba PE, Clubb RT J Biol Chem. 2014 Dec 12;289(50):34886-99. doi: 10.1074/jbc.M114.583013. Epub, 2014 Oct 14. PMID:25315777^[7]

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

References

↑ Newton SM, Klebba PE, Raynaud C, Shao Y, Jiang X, Dubail I, Archer C, Frehel C, Charbit A. The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron regulation and effect on virulence. Mol Microbiol. 2005 Feb;55(3):927-40. doi: 10.1111/j.1365-2958.2004.04436.x. PMID:15661014 doi:http://dx.doi.org/10.1111/j.1365-2958.2004.04436.x
↑ Xiao Q, Jiang X, Moore KJ, Shao Y, Pi H, Dubail I, Charbit A, Newton SM, Klebba PE. Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes. Mol Microbiol. 2011 Jun;80(6):1581-97. doi: 10.1111/j.1365-2958.2011.07667.x. , Epub 2011 May 6. PMID:21545655 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07667.x
↑ Malmirchegini GR, Sjodt M, Shnitkind S, Sawaya MR, Rosinski J, Newton SM, Klebba PE, Clubb RT. Novel Mechanism of Hemin Capture by Hbp2, the Hemoglobin-binding Hemophore from Listeria monocytogenes. J Biol Chem. 2014 Dec 12;289(50):34886-99. doi: 10.1074/jbc.M114.583013. Epub, 2014 Oct 14. PMID:25315777 doi:http://dx.doi.org/10.1074/jbc.M114.583013
↑ Newton SM, Klebba PE, Raynaud C, Shao Y, Jiang X, Dubail I, Archer C, Frehel C, Charbit A. The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron regulation and effect on virulence. Mol Microbiol. 2005 Feb;55(3):927-40. doi: 10.1111/j.1365-2958.2004.04436.x. PMID:15661014 doi:http://dx.doi.org/10.1111/j.1365-2958.2004.04436.x
↑ Xiao Q, Jiang X, Moore KJ, Shao Y, Pi H, Dubail I, Charbit A, Newton SM, Klebba PE. Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes. Mol Microbiol. 2011 Jun;80(6):1581-97. doi: 10.1111/j.1365-2958.2011.07667.x. , Epub 2011 May 6. PMID:21545655 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07667.x
↑ Malmirchegini GR, Sjodt M, Shnitkind S, Sawaya MR, Rosinski J, Newton SM, Klebba PE, Clubb RT. Novel Mechanism of Hemin Capture by Hbp2, the Hemoglobin-binding Hemophore from Listeria monocytogenes. J Biol Chem. 2014 Dec 12;289(50):34886-99. doi: 10.1074/jbc.M114.583013. Epub, 2014 Oct 14. PMID:25315777 doi:http://dx.doi.org/10.1074/jbc.M114.583013
↑ Malmirchegini GR, Sjodt M, Shnitkind S, Sawaya MR, Rosinski J, Newton SM, Klebba PE, Clubb RT. Novel Mechanism of Hemin Capture by Hbp2, the Hemoglobin-binding Hemophore from Listeria monocytogenes. J Biol Chem. 2014 Dec 12;289(50):34886-99. doi: 10.1074/jbc.M114.583013. Epub, 2014 Oct 14. PMID:25315777 doi:http://dx.doi.org/10.1074/jbc.M114.583013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4myp"

Categories: Large Structures | Listeria monocytogenes | Clubb RT | Malmirchegini GR | Sawaya MR

@@ Line 3: / Line 3: @@
 <StructureSection load='4myp' size='340' side='right'caption='[[4myp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4myp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MYP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4myp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MYP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BN418_2635, lmo2185 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</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=4myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myp OCA], [https://pdbe.org/4myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4myp RCSB], [https://www.ebi.ac.uk/pdbsum/4myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4myp ProSAT]</span></td></tr>
-<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=4myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myp OCA], [http://pdbe.org/4myp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4myp RCSB], [http://www.ebi.ac.uk/pdbsum/4myp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4myp ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HBP2_LISMO HBP2_LISMO] Acts as an extracellular and cell wall-bound hemophore; scavenges host heme and hemoglobin from the environment and also serves as a cell wall receptor for both (Probable). At low hemin (Hn) and hemoglobin (Hb) concentrations adsorbs Hn/Hb and presumably directs it to membrane transporters (Probable). Soluble Hbp2 can probably pass Hn/Hb to cell wall-anchored Hbp2, and both forms can accept Hn/Hb from Hbp1 (PubMed:25315777). May be involved in crossing the digestive barrier in infected animals (PubMed:15661014). Binds host hemin (Probable) (PubMed:21545655, PubMed:25315777). Binds host hemoglobin with affinity in the nanomolar range (PubMed:25315777).<ref>PMID:15661014</ref> <ref>PMID:21545655</ref> <ref>PMID:25315777</ref> <ref>PMID:15661014</ref> <ref>PMID:21545655</ref> <ref>PMID:25315777</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium monocytogenes hominis nyfeldt 1932]]
 [[Category: Large Structures]]
-[[Category: Clubb, R T]]
+[[Category: Listeria monocytogenes]]
-[[Category: Malmirchegini, G R]]
+[[Category: Clubb RT]]
-[[Category: Sawaya, M R]]
+[[Category: Malmirchegini GR]]
-[[Category: Hbp]]
+[[Category: Sawaya MR]]
-[[Category: Hbp2]]
-[[Category: Heme]]
-[[Category: Heme-binding protein]]
-[[Category: Hemoglobin]]
-[[Category: Listeria]]
-[[Category: N2]]
-[[Category: Neat domain]]

4myp

From Proteopedia

Revision as of 10:20, 28 December 2022

Structure of the central NEAT domain, N2, of the listerial Hbp2 protein complexed with heme

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox