1rwl

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(New page: 200px<br /><applet load="1rwl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwl, resolution 1.9&Aring;" /> '''Extracellular domain ...)
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[[Image:1rwl.jpg|left|200px]]<br /><applet load="1rwl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rwl, resolution 1.9&Aring;" />
caption="1rwl, resolution 1.9&Aring;" />
'''Extracellular domain of Mycobacterium tuberculosis PknD'''<br />
'''Extracellular domain of Mycobacterium tuberculosis PknD'''<br />
==Overview==
==Overview==
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Diverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein, kinases (STPKs), but little is known about the signals mediated by these, "eukaryotic-like" proteins. To explore the basis for signaling in the, bacterial STPK receptor family, we determined the structure of the sensor, domain of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD, sensor domain forms a rigid, six-bladed beta-propeller with a flexible, tether to the transmembrane domain. The PknD sensor domain is the most, symmetric beta-propeller structure described. All residues that vary most, among the blade subdomains cluster in the large "cup" motif, analogous to, the ligand-binding surface in many beta-propeller proteins. These results, suggest that PknD binds a multivalent ligand that signals by changing the, quaternary structure of the intracellular kinase domain.
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Diverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein kinases (STPKs), but little is known about the signals mediated by these "eukaryotic-like" proteins. To explore the basis for signaling in the bacterial STPK receptor family, we determined the structure of the sensor domain of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD sensor domain forms a rigid, six-bladed beta-propeller with a flexible tether to the transmembrane domain. The PknD sensor domain is the most symmetric beta-propeller structure described. All residues that vary most among the blade subdomains cluster in the large "cup" motif, analogous to the ligand-binding surface in many beta-propeller proteins. These results suggest that PknD binds a multivalent ligand that signals by changing the quaternary structure of the intracellular kinase domain.
==About this Structure==
==About this Structure==
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1RWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RWL OCA].
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1RWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWL OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alber, T.]]
[[Category: Alber, T.]]
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[[Category: Good, M.C.]]
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[[Category: Good, M C.]]
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[[Category: Greenstein, A.E.]]
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[[Category: Greenstein, A E.]]
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[[Category: Ng, H.L.]]
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[[Category: Ng, H L.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Young, T.A.]]
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[[Category: Young, T A.]]
[[Category: CD]]
[[Category: CD]]
[[Category: beta propeller]]
[[Category: beta propeller]]
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[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:54:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:17 2008''

Revision as of 12:55, 21 February 2008


1rwl, resolution 1.9Å

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Extracellular domain of Mycobacterium tuberculosis PknD

Overview

Diverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein kinases (STPKs), but little is known about the signals mediated by these "eukaryotic-like" proteins. To explore the basis for signaling in the bacterial STPK receptor family, we determined the structure of the sensor domain of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD sensor domain forms a rigid, six-bladed beta-propeller with a flexible tether to the transmembrane domain. The PknD sensor domain is the most symmetric beta-propeller structure described. All residues that vary most among the blade subdomains cluster in the large "cup" motif, analogous to the ligand-binding surface in many beta-propeller proteins. These results suggest that PknD binds a multivalent ligand that signals by changing the quaternary structure of the intracellular kinase domain.

About this Structure

1RWL is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller., Good MC, Greenstein AE, Young TA, Ng HL, Alber T, J Mol Biol. 2004 May 28;339(2):459-69. PMID:15136047

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