5d1z

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==IsdB NEAT1 bound by clone D4-10==
==IsdB NEAT1 bound by clone D4-10==
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<StructureSection load='5d1z' size='340' side='right' caption='[[5d1z]], [[Resolution|resolution]] 3.17&Aring;' scene=''>
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<StructureSection load='5d1z' size='340' side='right'caption='[[5d1z]], [[Resolution|resolution]] 3.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d1z]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d1z]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MSSA476 Staphylococcus aureus subsp. aureus MSSA476]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D1Z FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1x|5d1x]], [[5diq|5diq]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17&#8491;</td></tr>
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<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=5d1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1z OCA], [http://pdbe.org/5d1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1z RCSB], [http://www.ebi.ac.uk/pdbsum/5d1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1z ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1z OCA], [https://pdbe.org/5d1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d1z RCSB], [https://www.ebi.ac.uk/pdbsum/5d1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ISDB_STAAS ISDB_STAAS]] Seems to function as the primary receptor for hemoglobin since its inactivation inhibits the ability of S.aureus to bind hemoglobin. Binds hemoglobin in a dose-dependent way. Required for S.aureus growth using hemoglobin as the sole iron source. Also required for virulence. IsdA and/or IsdB promote resistance to hydrogen peroxide and killing by neutrophils (By similarity).
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[https://www.uniprot.org/uniprot/CDCA2_HUMAN CDCA2_HUMAN] Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates.<ref>PMID:16492807</ref> <ref>PMID:16998479</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Staphylococcus aureus is both an important pathogen and a human commensal. To explore this ambivalent relationship between host and microbe, we analysed the memory humoral response against IsdB, a protein involved in iron acquisition, in four healthy donors. Here we show that in all donors a heavily biased use of two immunoglobulin heavy chain germlines generated high affinity (pM) antibodies that neutralize the two IsdB NEAT domains, IGHV4-39 for NEAT1 and IGHV1-69 for NEAT2. In contrast to the typical antibody/antigen interactions, the binding is primarily driven by the germline-encoded hydrophobic CDRH-2 motifs of IGHV1-69 and IGHV4-39, with a binding mechanism nearly identical for each antibody derived from different donors. Our results suggest that IGHV1-69 and IGHV4-39, while part of the adaptive immune system, may have evolved under selection pressure to encode a binding motif innately capable of recognizing and neutralizing a structurally conserved protein domain involved in pathogen iron acquisition.
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Germline-encoded neutralization of a Staphylococcus aureus virulence factor by the human antibody repertoire.,Yeung YA, Foletti D, Deng X, Abdiche Y, Strop P, Glanville J, Pitts S, Lindquist K, Sundar PD, Sirota M, Hasa-Moreno A, Pham A, Melton Witt J, Ni I, Pons J, Shelton D, Rajpal A, Chaparro-Riggers J Nat Commun. 2016 Nov 18;7:13376. doi: 10.1038/ncomms13376. PMID:27857134<ref>PMID:27857134</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5d1z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Deng, X]]
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[[Category: Homo sapiens]]
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[[Category: Germline encoded]]
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[[Category: Large Structures]]
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[[Category: Immune system]]
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[[Category: Staphylococcus aureus subsp. aureus MSSA476]]
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[[Category: Isdb]]
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[[Category: Deng X]]
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[[Category: Neat1]]
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Current revision

IsdB NEAT1 bound by clone D4-10

PDB ID 5d1z

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