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.


2o6d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o6d.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2o6d.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o6d| PDB=2o6d | SCENE= }}
{{STRUCTURE_2o6d| PDB=2o6d | SCENE= }}
-
'''Structure of native rTp34 from Treponema pallidum'''
+
===Structure of native rTp34 from Treponema pallidum===
-
==Overview==
+
<!--
-
The Tp34 (TP0971) membrane lipoprotein of Treponema pallidum, an obligate human pathogen and the agent of syphilis, was previously reported to have lactoferrin binding properties. Given the non-cultivatable nature of T. pallidum, a structure-to-function approach was pursued to clarify further potential relationships between the Tp34 structural and biochemical properties and its propensity to bind human lactoferrin. The crystal structure of a nonacylated, recombinant form of Tp34 (rTp34), solved to a resolution of 1.9A(,) revealed two metaloccupied binding sites within a dimer; the identity of the ion most likely was zinc. Residues from both of the monomers contributed to the interfacial metal-binding sites; a novel feature was that the delta-sulfur of methionine coordinated the zinc ion. Analytical ultracentrifugation showed that, in solution, rTp34 formed a metal-stabilized dimer and that rTp34 bound human lactoferrin with a stoichiometry of 2:1. Isothermal titration calorimetry further revealed that rTp34 bound human lactoferrin at high (submicromolar) affinity. Finally, membrane topology studies revealed that native Tp34 is not located on the outer surface (outer membrane) of T. pallidum but, rather, is periplasmic. How propensity of Tp34 to bind zinc and the iron-sequestering lactoferrin may relate overall to the biology of T. pallidum infection in humans is discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17192261}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17192261 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17192261}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Metal-ion binding]]
[[Category: Metal-ion binding]]
[[Category: Syphili]]
[[Category: Syphili]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:22:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:39:13 2008''

Revision as of 10:39, 29 July 2008

Image:2o6d.png

Template:STRUCTURE 2o6d

Structure of native rTp34 from Treponema pallidum

Template:ABSTRACT PUBMED 17192261

About this Structure

2O6D is a Single protein structure of sequence from Treponema pallidum. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin., Deka RK, Brautigam CA, Tomson FL, Lumpkins SB, Tomchick DR, Machius M, Norgard MV, J Biol Chem. 2007 Feb 23;282(8):5944-58. Epub 2006 Dec 27. PMID:17192261

Page seeded by OCA on Tue Jul 29 13:39:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o6d"
Personal tools