2itf
From Proteopedia
(New page: 200px<br /><applet load="2itf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2itf, resolution 1.900Å" /> '''Crystal structure I...) |
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| - | [[Image:2itf.jpg|left|200px]]<br /><applet load="2itf" size=" | + | [[Image:2itf.jpg|left|200px]]<br /><applet load="2itf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2itf, resolution 1.900Å" /> | caption="2itf, resolution 1.900Å" /> | ||
'''Crystal structure IsdA NEAT domain from Staphylococcus aureus with heme bound'''<br /> | '''Crystal structure IsdA NEAT domain from Staphylococcus aureus with heme bound'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Successful pathogenic organisms have developed mechanisms to thrive under | + | Successful pathogenic organisms have developed mechanisms to thrive under extreme levels of iron restriction. Haem-iron represents the largest iron reservoir in the human body and is a significant source of iron for some bacterial pathogens. NEAT (NEAr Transporter) domains are found exclusively in a family of cell surface proteins in Gram-positive bacteria. Many NEAT domain-containing proteins, including IsdA in Staphylococcus aureus, are implicated in haem binding. Here, we show that overexpression of IsdA in S. aureus enhances growth and an inactivation mutant of IsdA has a growth defect, compared with wild type, when grown in media containing haem as the sole iron source. Furthermore, the haem-binding property of IsdA is contained within the NEAT domain. Crystal structures of the apo-IsdA NEAT domain and in complex with haem were solved and reveal a clathrin adapter-like beta-sandwich fold with a large hydrophobic haem-binding pocket. Haem is bound with the propionate groups directed at the molecular surface and the iron is co-ordinated solely by Tyr(166). The phenol groups of Tyr(166) and Tyr(170) form an H-bond that may function in regulating haem binding and release. An analysis of IsdA structure-sequence alignments indicate that conservation of Tyr(166) is a predictor of haem binding by NEAT domains. |
==About this Structure== | ==About this Structure== | ||
| - | 2ITF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2ITF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Grigg, J | + | [[Category: Grigg, J C.]] |
| - | [[Category: Heinrichs, D | + | [[Category: Heinrichs, D E.]] |
| - | [[Category: Murphy, M | + | [[Category: Murphy, M E.]] |
| - | [[Category: Vermeiren, C | + | [[Category: Vermeiren, C L.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: heme]] | [[Category: heme]] | ||
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[[Category: neat domain]] | [[Category: neat domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:47 2008'' |
Revision as of 15:55, 21 February 2008
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Crystal structure IsdA NEAT domain from Staphylococcus aureus with heme bound
Overview
Successful pathogenic organisms have developed mechanisms to thrive under extreme levels of iron restriction. Haem-iron represents the largest iron reservoir in the human body and is a significant source of iron for some bacterial pathogens. NEAT (NEAr Transporter) domains are found exclusively in a family of cell surface proteins in Gram-positive bacteria. Many NEAT domain-containing proteins, including IsdA in Staphylococcus aureus, are implicated in haem binding. Here, we show that overexpression of IsdA in S. aureus enhances growth and an inactivation mutant of IsdA has a growth defect, compared with wild type, when grown in media containing haem as the sole iron source. Furthermore, the haem-binding property of IsdA is contained within the NEAT domain. Crystal structures of the apo-IsdA NEAT domain and in complex with haem were solved and reveal a clathrin adapter-like beta-sandwich fold with a large hydrophobic haem-binding pocket. Haem is bound with the propionate groups directed at the molecular surface and the iron is co-ordinated solely by Tyr(166). The phenol groups of Tyr(166) and Tyr(170) form an H-bond that may function in regulating haem binding and release. An analysis of IsdA structure-sequence alignments indicate that conservation of Tyr(166) is a predictor of haem binding by NEAT domains.
About this Structure
2ITF is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.
Reference
Haem recognition by a Staphylococcus aureus NEAT domain., Grigg JC, Vermeiren CL, Heinrichs DE, Murphy ME, Mol Microbiol. 2007 Jan;63(1):139-49. PMID:17229211
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