2bmm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2bmm.gif|left|200px]]
{{Seed}}
[[Image:2bmm.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bmm|  PDB=2bmm  |  SCENE=  }}  
{{STRUCTURE_2bmm|  PDB=2bmm  |  SCENE=  }}  


'''X-RAY STRUCTURE OF A NOVEL THERMOSTABLE HEMOGLOBIN FROM THE ACTINOBACTERIUM THERMOBIFIDA FUSCA'''
===X-RAY STRUCTURE OF A NOVEL THERMOSTABLE HEMOGLOBIN FROM THE ACTINOBACTERIUM THERMOBIFIDA FUSCA===




==Overview==
<!--  
The gene coding for a hemoglobin-like protein (Tf-trHb) has been identified in the thermophilic actinobacterium Thermobifida fusca and cloned in Escherichia coli for overexpression. The crystal structure of the ferric, acetate-bound derivative, was obtained at 2.48 A resolution. The three-dimensional structure of Tf-trHb is similar to structures reported for the truncated hemoglobins from Mycobacterium tuberculosis and Bacillus subtilis in its central domain. The complete lack of diffraction patterns relative to the N- and C-terminal segments indicates that these are unstructured polypeptides chains, consistent with their facile cleavage in solution. The absence of internal cavities and the presence of two water molecules between the bound acetate ion and the protein surface suggest that the mode of ligand entry is similar to that of typical hemoglobins. The protein is characterized by higher thermostability than the similar mesophilic truncated hemoglobin from B. subtilis, as demonstrated by far-UV CD melting experiments on the cyano-met derivatives. The ligand-binding properties of Tf-trHb, analyzed in stopped flow experiments, demonstrate that Tf-trHb is capable of efficient O2 binding and release between 55 and 60 degrees C, the optimal growth temperature for Thermobifida fusca.
The line below this paragraph, {{ABSTRACT_PUBMED_16098200}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16098200 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16098200}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Oxygen storage/transport]]
[[Category: Oxygen storage/transport]]
[[Category: Thermostable protein]]
[[Category: Thermostable protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:30:10 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:12:47 2008''

Revision as of 06:12, 29 July 2008

File:2bmm.png

Template:STRUCTURE 2bmm

X-RAY STRUCTURE OF A NOVEL THERMOSTABLE HEMOGLOBIN FROM THE ACTINOBACTERIUM THERMOBIFIDA FUSCA

Template:ABSTRACT PUBMED 16098200

About this Structure

2BMM is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.

Reference

A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca., Bonamore A, Ilari A, Giangiacomo L, Bellelli A, Morea V, Boffi A, FEBS J. 2005 Aug;272(16):4189-201. PMID:16098200

Page seeded by OCA on Tue Jul 29 09:12:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2bmm&oldid=736137"