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| - | [[Image:1hqb.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hqb| PDB=1hqb | SCENE= }} | | {{STRUCTURE_1hqb| PDB=1hqb | SCENE= }} |
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| - | '''TERTIARY STRUCTURE OF APO-D-ALANYL CARRIER PROTEIN'''
| + | ===TERTIARY STRUCTURE OF APO-D-ALANYL CARRIER PROTEIN=== |
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| - | ==Overview==
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| - | The D-alanylation of lipoteichoic acid (LTA) allows the Gram-positive organism to modulate its surface charge, regulate ligand binding, and control the electromechanical properties of the cell wall. The incorporation of D-alanine into LTA requires the D-alanine:D-alanyl carrier protein ligase (AMP-forming) (Dcl) and the carrier protein (Dcp). The high-resolution solution structure of the 81-residue (8.9 kDa) Dcp has been determined by multidimensional heteronuclear NMR. An ensemble of 30 structures was calculated using the torsion angle dynamics approach of DYANA. These calculations utilized 3288 NOEs containing 1582 unique nontrivial NOE distance constraints. Superposition of residues 4-81 on the mean structure yields average atomic rmsd values of 0.43 +/- 0.08 and 0.86 +/- 0.09 A for backbone and non-hydrogen atoms, respectively. The solution structure is composed of three alpha-helices in a bundle with additional short 3(10)- and alpha-helices in intervening loops. Comparisons of the three-dimensional structure with the acyl carrier proteins involved in fatty acid, polyketide, and nonribosomal peptide syntheses support the conclusion that Dcp is a homologue in this family. While there is conservation of the three-helix bundle fold, Dcp has a higher enthalpy of unfolding and no apparent divalent metal binding site(s), features that distinguish it from the fatty acid synthase acyl carrier protein of Escherichia coli. This three-dimensional structure also provides insights into the D-alanine ligation site recognized by Dcl, as well as the site which may bind the poly(glycerophosphate) acceptor moiety of membrane-associated LTA. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11434765}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11434765 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11434765}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1HQB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQB OCA]. | + | 1HQB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQB OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Zhang, Q.]] | | [[Category: Zhang, Q.]] |
| | [[Category: 3-helix bundle]] | | [[Category: 3-helix bundle]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:07:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:31:55 2008'' |
Revision as of 05:31, 1 July 2008
Template:STRUCTURE 1hqb
TERTIARY STRUCTURE OF APO-D-ALANYL CARRIER PROTEIN
Template:ABSTRACT PUBMED 11434765
About this Structure
1HQB is a Single protein structure of sequence from Lactobacillus casei. Full experimental information is available from OCA.
Reference
Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein., Volkman BF, Zhang Q, Debabov DV, Rivera E, Kresheck GC, Neuhaus FC, Biochemistry. 2001 Jul 10;40(27):7964-72. PMID:11434765
Page seeded by OCA on Tue Jul 1 08:31:55 2008
